The TRAPP complex mediates secretion arrest induced by stress granule assembly
Abstract The TRAnsport Protein Particle (TRAPP) complex controls multiple membrane trafficking steps and is strategically positioned to mediate cell adaptation to diverse environmental conditions, including acute stress. We have identified the TRAPP complex as a component of a branch of the integrat...
Ausführliche Beschreibung
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| Autor*in: |
Zappa, Francesca [verfasserIn] Wilson, Cathal [verfasserIn] Di Tullio, Giuseppe [verfasserIn] Santoro, Michele [verfasserIn] Pucci, Piero [verfasserIn] Monti, Maria [verfasserIn] D'Amico, Davide [verfasserIn] Pisonero‐Vaquero, Sandra [verfasserIn] De Cegli, Rossella [verfasserIn] Romano, Alessia [verfasserIn] Saleem, Moin A [verfasserIn] Polishchuk, Elena [verfasserIn] Failli, Mario [verfasserIn] Giaquinto, Laura [verfasserIn] De Matteis, Maria Antonietta [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2019 |
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| Schlagwörter: |
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| Anmerkung: |
© The Author(s) 2019 |
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| Übergeordnetes Werk: |
Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 38(2019), 19 vom: 20. Aug. |
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| Übergeordnetes Werk: |
volume:38 ; year:2019 ; number:19 ; day:20 ; month:08 |
| Links: |
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| DOI / URN: |
10.15252/embj.2019101704 |
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| Katalog-ID: |
SPR05801635X |
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| 041 | |a eng | ||
| 100 | 1 | |a Zappa, Francesca |e verfasserin |0 (orcid)0000-0003-1263-3828 |4 aut | |
| 245 | 1 | 0 | |a The TRAPP complex mediates secretion arrest induced by stress granule assembly |
| 264 | 1 | |c 2019 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a Computermedien |b c |2 rdamedia | ||
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| 500 | |a © The Author(s) 2019 | ||
| 520 | |a Abstract The TRAnsport Protein Particle (TRAPP) complex controls multiple membrane trafficking steps and is strategically positioned to mediate cell adaptation to diverse environmental conditions, including acute stress. We have identified the TRAPP complex as a component of a branch of the integrated stress response that impinges on the early secretory pathway. The TRAPP complex associates with and drives the recruitment of the COPII coat to stress granules (SGs) leading to vesiculation of the Golgi complex and arrest of ER export. The relocation of the TRAPP complex and COPII to SGs only occurs in cycling cells and is CDK1/2‐dependent, being driven by the interaction of TRAPP with hnRNPK, a CDK substrate that associates with SGs when phosphorylated. In addition, CDK1/2 inhibition impairs TRAPP complex/COPII relocation to SGs while stabilizing them at ER exit sites. Importantly, the TRAPP complex controls the maturation of SGs. SGs that assemble in TRAPP‐depleted cells are smaller and are no longer able to recruit RACK1 and Raptor, two TRAPP‐interactive signaling proteins, sensitizing cells to stress‐induced apoptosis. | ||
| 520 | |a Synopsis The TRAnsport Protein Particle (TRAPP) complex, which controls multiple membrane trafficking steps along the secretory pathway, mediates cellular adaptation to acute stress by associating with and driving the recruitment of the COPII coat to stress granules (SGs), thereby halting secretion and possibly limiting energy consumption. The TRAPP complex associates with and drives the recruitment of the COPII coat to SGs.The TRAPP complex promotes the maturation of SGs.Relocation of TRAPP complex and COPII to SGs depends on CDK1/2 and occurs only in cycling cells.Association of TRAPP complex and COPII with SGs halts secretion. | ||
| 520 | |a Graphical Abstract TRAPP‐dependent stress granule recruitment of COPII vesicle coats to halt secretion and limit energy consumption is involved in cellular adapation to acute stress. | ||
| 650 | 4 | |a Cdk |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a COPII |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a integrated stress response |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a stress granules |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a TRAPP complex |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Wilson, Cathal |e verfasserin |4 aut | |
| 700 | 1 | |a Di Tullio, Giuseppe |e verfasserin |4 aut | |
| 700 | 1 | |a Santoro, Michele |e verfasserin |4 aut | |
| 700 | 1 | |a Pucci, Piero |e verfasserin |4 aut | |
| 700 | 1 | |a Monti, Maria |e verfasserin |4 aut | |
| 700 | 1 | |a D'Amico, Davide |e verfasserin |4 aut | |
| 700 | 1 | |a Pisonero‐Vaquero, Sandra |e verfasserin |4 aut | |
| 700 | 1 | |a De Cegli, Rossella |e verfasserin |4 aut | |
| 700 | 1 | |a Romano, Alessia |e verfasserin |4 aut | |
| 700 | 1 | |a Saleem, Moin A |e verfasserin |4 aut | |
| 700 | 1 | |a Polishchuk, Elena |e verfasserin |4 aut | |
| 700 | 1 | |a Failli, Mario |e verfasserin |4 aut | |
| 700 | 1 | |a Giaquinto, Laura |e verfasserin |4 aut | |
| 700 | 1 | |a De Matteis, Maria Antonietta |e verfasserin |0 (orcid)0000-0003-0053-3061 |4 aut | |
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10.15252/embj.2019101704 doi (DE-627)SPR05801635X (SPR)embj.2019101704-e DE-627 ger DE-627 rakwb eng Zappa, Francesca verfasserin (orcid)0000-0003-1263-3828 aut The TRAPP complex mediates secretion arrest induced by stress granule assembly 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Abstract The TRAnsport Protein Particle (TRAPP) complex controls multiple membrane trafficking steps and is strategically positioned to mediate cell adaptation to diverse environmental conditions, including acute stress. We have identified the TRAPP complex as a component of a branch of the integrated stress response that impinges on the early secretory pathway. The TRAPP complex associates with and drives the recruitment of the COPII coat to stress granules (SGs) leading to vesiculation of the Golgi complex and arrest of ER export. The relocation of the TRAPP complex and COPII to SGs only occurs in cycling cells and is CDK1/2‐dependent, being driven by the interaction of TRAPP with hnRNPK, a CDK substrate that associates with SGs when phosphorylated. In addition, CDK1/2 inhibition impairs TRAPP complex/COPII relocation to SGs while stabilizing them at ER exit sites. Importantly, the TRAPP complex controls the maturation of SGs. SGs that assemble in TRAPP‐depleted cells are smaller and are no longer able to recruit RACK1 and Raptor, two TRAPP‐interactive signaling proteins, sensitizing cells to stress‐induced apoptosis. Synopsis The TRAnsport Protein Particle (TRAPP) complex, which controls multiple membrane trafficking steps along the secretory pathway, mediates cellular adaptation to acute stress by associating with and driving the recruitment of the COPII coat to stress granules (SGs), thereby halting secretion and possibly limiting energy consumption. The TRAPP complex associates with and drives the recruitment of the COPII coat to SGs.The TRAPP complex promotes the maturation of SGs.Relocation of TRAPP complex and COPII to SGs depends on CDK1/2 and occurs only in cycling cells.Association of TRAPP complex and COPII with SGs halts secretion. Graphical Abstract TRAPP‐dependent stress granule recruitment of COPII vesicle coats to halt secretion and limit energy consumption is involved in cellular adapation to acute stress. Cdk (dpeaa)DE-He213 COPII (dpeaa)DE-He213 integrated stress response (dpeaa)DE-He213 stress granules (dpeaa)DE-He213 TRAPP complex (dpeaa)DE-He213 Wilson, Cathal verfasserin aut Di Tullio, Giuseppe verfasserin aut Santoro, Michele verfasserin aut Pucci, Piero verfasserin aut Monti, Maria verfasserin aut D'Amico, Davide verfasserin aut Pisonero‐Vaquero, Sandra verfasserin aut De Cegli, Rossella verfasserin aut Romano, Alessia verfasserin aut Saleem, Moin A verfasserin aut Polishchuk, Elena verfasserin aut Failli, Mario verfasserin aut Giaquinto, Laura verfasserin aut De Matteis, Maria Antonietta verfasserin (orcid)0000-0003-0053-3061 aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 38(2019), 19 vom: 20. Aug. (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:38 year:2019 number:19 day:20 month:08 https://dx.doi.org/10.15252/embj.2019101704 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 38 2019 19 20 08 |
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10.15252/embj.2019101704 doi (DE-627)SPR05801635X (SPR)embj.2019101704-e DE-627 ger DE-627 rakwb eng Zappa, Francesca verfasserin (orcid)0000-0003-1263-3828 aut The TRAPP complex mediates secretion arrest induced by stress granule assembly 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Abstract The TRAnsport Protein Particle (TRAPP) complex controls multiple membrane trafficking steps and is strategically positioned to mediate cell adaptation to diverse environmental conditions, including acute stress. We have identified the TRAPP complex as a component of a branch of the integrated stress response that impinges on the early secretory pathway. The TRAPP complex associates with and drives the recruitment of the COPII coat to stress granules (SGs) leading to vesiculation of the Golgi complex and arrest of ER export. The relocation of the TRAPP complex and COPII to SGs only occurs in cycling cells and is CDK1/2‐dependent, being driven by the interaction of TRAPP with hnRNPK, a CDK substrate that associates with SGs when phosphorylated. In addition, CDK1/2 inhibition impairs TRAPP complex/COPII relocation to SGs while stabilizing them at ER exit sites. Importantly, the TRAPP complex controls the maturation of SGs. SGs that assemble in TRAPP‐depleted cells are smaller and are no longer able to recruit RACK1 and Raptor, two TRAPP‐interactive signaling proteins, sensitizing cells to stress‐induced apoptosis. Synopsis The TRAnsport Protein Particle (TRAPP) complex, which controls multiple membrane trafficking steps along the secretory pathway, mediates cellular adaptation to acute stress by associating with and driving the recruitment of the COPII coat to stress granules (SGs), thereby halting secretion and possibly limiting energy consumption. The TRAPP complex associates with and drives the recruitment of the COPII coat to SGs.The TRAPP complex promotes the maturation of SGs.Relocation of TRAPP complex and COPII to SGs depends on CDK1/2 and occurs only in cycling cells.Association of TRAPP complex and COPII with SGs halts secretion. Graphical Abstract TRAPP‐dependent stress granule recruitment of COPII vesicle coats to halt secretion and limit energy consumption is involved in cellular adapation to acute stress. Cdk (dpeaa)DE-He213 COPII (dpeaa)DE-He213 integrated stress response (dpeaa)DE-He213 stress granules (dpeaa)DE-He213 TRAPP complex (dpeaa)DE-He213 Wilson, Cathal verfasserin aut Di Tullio, Giuseppe verfasserin aut Santoro, Michele verfasserin aut Pucci, Piero verfasserin aut Monti, Maria verfasserin aut D'Amico, Davide verfasserin aut Pisonero‐Vaquero, Sandra verfasserin aut De Cegli, Rossella verfasserin aut Romano, Alessia verfasserin aut Saleem, Moin A verfasserin aut Polishchuk, Elena verfasserin aut Failli, Mario verfasserin aut Giaquinto, Laura verfasserin aut De Matteis, Maria Antonietta verfasserin (orcid)0000-0003-0053-3061 aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 38(2019), 19 vom: 20. Aug. (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:38 year:2019 number:19 day:20 month:08 https://dx.doi.org/10.15252/embj.2019101704 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 38 2019 19 20 08 |
| allfields_unstemmed |
10.15252/embj.2019101704 doi (DE-627)SPR05801635X (SPR)embj.2019101704-e DE-627 ger DE-627 rakwb eng Zappa, Francesca verfasserin (orcid)0000-0003-1263-3828 aut The TRAPP complex mediates secretion arrest induced by stress granule assembly 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Abstract The TRAnsport Protein Particle (TRAPP) complex controls multiple membrane trafficking steps and is strategically positioned to mediate cell adaptation to diverse environmental conditions, including acute stress. We have identified the TRAPP complex as a component of a branch of the integrated stress response that impinges on the early secretory pathway. The TRAPP complex associates with and drives the recruitment of the COPII coat to stress granules (SGs) leading to vesiculation of the Golgi complex and arrest of ER export. The relocation of the TRAPP complex and COPII to SGs only occurs in cycling cells and is CDK1/2‐dependent, being driven by the interaction of TRAPP with hnRNPK, a CDK substrate that associates with SGs when phosphorylated. In addition, CDK1/2 inhibition impairs TRAPP complex/COPII relocation to SGs while stabilizing them at ER exit sites. Importantly, the TRAPP complex controls the maturation of SGs. SGs that assemble in TRAPP‐depleted cells are smaller and are no longer able to recruit RACK1 and Raptor, two TRAPP‐interactive signaling proteins, sensitizing cells to stress‐induced apoptosis. Synopsis The TRAnsport Protein Particle (TRAPP) complex, which controls multiple membrane trafficking steps along the secretory pathway, mediates cellular adaptation to acute stress by associating with and driving the recruitment of the COPII coat to stress granules (SGs), thereby halting secretion and possibly limiting energy consumption. The TRAPP complex associates with and drives the recruitment of the COPII coat to SGs.The TRAPP complex promotes the maturation of SGs.Relocation of TRAPP complex and COPII to SGs depends on CDK1/2 and occurs only in cycling cells.Association of TRAPP complex and COPII with SGs halts secretion. Graphical Abstract TRAPP‐dependent stress granule recruitment of COPII vesicle coats to halt secretion and limit energy consumption is involved in cellular adapation to acute stress. Cdk (dpeaa)DE-He213 COPII (dpeaa)DE-He213 integrated stress response (dpeaa)DE-He213 stress granules (dpeaa)DE-He213 TRAPP complex (dpeaa)DE-He213 Wilson, Cathal verfasserin aut Di Tullio, Giuseppe verfasserin aut Santoro, Michele verfasserin aut Pucci, Piero verfasserin aut Monti, Maria verfasserin aut D'Amico, Davide verfasserin aut Pisonero‐Vaquero, Sandra verfasserin aut De Cegli, Rossella verfasserin aut Romano, Alessia verfasserin aut Saleem, Moin A verfasserin aut Polishchuk, Elena verfasserin aut Failli, Mario verfasserin aut Giaquinto, Laura verfasserin aut De Matteis, Maria Antonietta verfasserin (orcid)0000-0003-0053-3061 aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 38(2019), 19 vom: 20. Aug. (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:38 year:2019 number:19 day:20 month:08 https://dx.doi.org/10.15252/embj.2019101704 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 38 2019 19 20 08 |
| allfieldsGer |
10.15252/embj.2019101704 doi (DE-627)SPR05801635X (SPR)embj.2019101704-e DE-627 ger DE-627 rakwb eng Zappa, Francesca verfasserin (orcid)0000-0003-1263-3828 aut The TRAPP complex mediates secretion arrest induced by stress granule assembly 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Abstract The TRAnsport Protein Particle (TRAPP) complex controls multiple membrane trafficking steps and is strategically positioned to mediate cell adaptation to diverse environmental conditions, including acute stress. We have identified the TRAPP complex as a component of a branch of the integrated stress response that impinges on the early secretory pathway. The TRAPP complex associates with and drives the recruitment of the COPII coat to stress granules (SGs) leading to vesiculation of the Golgi complex and arrest of ER export. The relocation of the TRAPP complex and COPII to SGs only occurs in cycling cells and is CDK1/2‐dependent, being driven by the interaction of TRAPP with hnRNPK, a CDK substrate that associates with SGs when phosphorylated. In addition, CDK1/2 inhibition impairs TRAPP complex/COPII relocation to SGs while stabilizing them at ER exit sites. Importantly, the TRAPP complex controls the maturation of SGs. SGs that assemble in TRAPP‐depleted cells are smaller and are no longer able to recruit RACK1 and Raptor, two TRAPP‐interactive signaling proteins, sensitizing cells to stress‐induced apoptosis. Synopsis The TRAnsport Protein Particle (TRAPP) complex, which controls multiple membrane trafficking steps along the secretory pathway, mediates cellular adaptation to acute stress by associating with and driving the recruitment of the COPII coat to stress granules (SGs), thereby halting secretion and possibly limiting energy consumption. The TRAPP complex associates with and drives the recruitment of the COPII coat to SGs.The TRAPP complex promotes the maturation of SGs.Relocation of TRAPP complex and COPII to SGs depends on CDK1/2 and occurs only in cycling cells.Association of TRAPP complex and COPII with SGs halts secretion. Graphical Abstract TRAPP‐dependent stress granule recruitment of COPII vesicle coats to halt secretion and limit energy consumption is involved in cellular adapation to acute stress. Cdk (dpeaa)DE-He213 COPII (dpeaa)DE-He213 integrated stress response (dpeaa)DE-He213 stress granules (dpeaa)DE-He213 TRAPP complex (dpeaa)DE-He213 Wilson, Cathal verfasserin aut Di Tullio, Giuseppe verfasserin aut Santoro, Michele verfasserin aut Pucci, Piero verfasserin aut Monti, Maria verfasserin aut D'Amico, Davide verfasserin aut Pisonero‐Vaquero, Sandra verfasserin aut De Cegli, Rossella verfasserin aut Romano, Alessia verfasserin aut Saleem, Moin A verfasserin aut Polishchuk, Elena verfasserin aut Failli, Mario verfasserin aut Giaquinto, Laura verfasserin aut De Matteis, Maria Antonietta verfasserin (orcid)0000-0003-0053-3061 aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 38(2019), 19 vom: 20. Aug. (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:38 year:2019 number:19 day:20 month:08 https://dx.doi.org/10.15252/embj.2019101704 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 38 2019 19 20 08 |
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10.15252/embj.2019101704 doi (DE-627)SPR05801635X (SPR)embj.2019101704-e DE-627 ger DE-627 rakwb eng Zappa, Francesca verfasserin (orcid)0000-0003-1263-3828 aut The TRAPP complex mediates secretion arrest induced by stress granule assembly 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Abstract The TRAnsport Protein Particle (TRAPP) complex controls multiple membrane trafficking steps and is strategically positioned to mediate cell adaptation to diverse environmental conditions, including acute stress. We have identified the TRAPP complex as a component of a branch of the integrated stress response that impinges on the early secretory pathway. The TRAPP complex associates with and drives the recruitment of the COPII coat to stress granules (SGs) leading to vesiculation of the Golgi complex and arrest of ER export. The relocation of the TRAPP complex and COPII to SGs only occurs in cycling cells and is CDK1/2‐dependent, being driven by the interaction of TRAPP with hnRNPK, a CDK substrate that associates with SGs when phosphorylated. In addition, CDK1/2 inhibition impairs TRAPP complex/COPII relocation to SGs while stabilizing them at ER exit sites. Importantly, the TRAPP complex controls the maturation of SGs. SGs that assemble in TRAPP‐depleted cells are smaller and are no longer able to recruit RACK1 and Raptor, two TRAPP‐interactive signaling proteins, sensitizing cells to stress‐induced apoptosis. Synopsis The TRAnsport Protein Particle (TRAPP) complex, which controls multiple membrane trafficking steps along the secretory pathway, mediates cellular adaptation to acute stress by associating with and driving the recruitment of the COPII coat to stress granules (SGs), thereby halting secretion and possibly limiting energy consumption. The TRAPP complex associates with and drives the recruitment of the COPII coat to SGs.The TRAPP complex promotes the maturation of SGs.Relocation of TRAPP complex and COPII to SGs depends on CDK1/2 and occurs only in cycling cells.Association of TRAPP complex and COPII with SGs halts secretion. Graphical Abstract TRAPP‐dependent stress granule recruitment of COPII vesicle coats to halt secretion and limit energy consumption is involved in cellular adapation to acute stress. Cdk (dpeaa)DE-He213 COPII (dpeaa)DE-He213 integrated stress response (dpeaa)DE-He213 stress granules (dpeaa)DE-He213 TRAPP complex (dpeaa)DE-He213 Wilson, Cathal verfasserin aut Di Tullio, Giuseppe verfasserin aut Santoro, Michele verfasserin aut Pucci, Piero verfasserin aut Monti, Maria verfasserin aut D'Amico, Davide verfasserin aut Pisonero‐Vaquero, Sandra verfasserin aut De Cegli, Rossella verfasserin aut Romano, Alessia verfasserin aut Saleem, Moin A verfasserin aut Polishchuk, Elena verfasserin aut Failli, Mario verfasserin aut Giaquinto, Laura verfasserin aut De Matteis, Maria Antonietta verfasserin (orcid)0000-0003-0053-3061 aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 38(2019), 19 vom: 20. Aug. (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:38 year:2019 number:19 day:20 month:08 https://dx.doi.org/10.15252/embj.2019101704 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 38 2019 19 20 08 |
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Zappa, Francesca @@aut@@ Wilson, Cathal @@aut@@ Di Tullio, Giuseppe @@aut@@ Santoro, Michele @@aut@@ Pucci, Piero @@aut@@ Monti, Maria @@aut@@ D'Amico, Davide @@aut@@ Pisonero‐Vaquero, Sandra @@aut@@ De Cegli, Rossella @@aut@@ Romano, Alessia @@aut@@ Saleem, Moin A @@aut@@ Polishchuk, Elena @@aut@@ Failli, Mario @@aut@@ Giaquinto, Laura @@aut@@ De Matteis, Maria Antonietta @@aut@@ |
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Zappa, Francesca |
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Zappa, Francesca misc Cdk misc COPII misc integrated stress response misc stress granules misc TRAPP complex The TRAPP complex mediates secretion arrest induced by stress granule assembly |
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The TRAPP complex mediates secretion arrest induced by stress granule assembly Cdk (dpeaa)DE-He213 COPII (dpeaa)DE-He213 integrated stress response (dpeaa)DE-He213 stress granules (dpeaa)DE-He213 TRAPP complex (dpeaa)DE-He213 |
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The TRAPP complex mediates secretion arrest induced by stress granule assembly |
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The TRAPP complex mediates secretion arrest induced by stress granule assembly |
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Zappa, Francesca Wilson, Cathal Di Tullio, Giuseppe Santoro, Michele Pucci, Piero Monti, Maria D'Amico, Davide Pisonero‐Vaquero, Sandra De Cegli, Rossella Romano, Alessia Saleem, Moin A Polishchuk, Elena Failli, Mario Giaquinto, Laura De Matteis, Maria Antonietta |
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the trapp complex mediates secretion arrest induced by stress granule assembly |
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The TRAPP complex mediates secretion arrest induced by stress granule assembly |
| abstract |
Abstract The TRAnsport Protein Particle (TRAPP) complex controls multiple membrane trafficking steps and is strategically positioned to mediate cell adaptation to diverse environmental conditions, including acute stress. We have identified the TRAPP complex as a component of a branch of the integrated stress response that impinges on the early secretory pathway. The TRAPP complex associates with and drives the recruitment of the COPII coat to stress granules (SGs) leading to vesiculation of the Golgi complex and arrest of ER export. The relocation of the TRAPP complex and COPII to SGs only occurs in cycling cells and is CDK1/2‐dependent, being driven by the interaction of TRAPP with hnRNPK, a CDK substrate that associates with SGs when phosphorylated. In addition, CDK1/2 inhibition impairs TRAPP complex/COPII relocation to SGs while stabilizing them at ER exit sites. Importantly, the TRAPP complex controls the maturation of SGs. SGs that assemble in TRAPP‐depleted cells are smaller and are no longer able to recruit RACK1 and Raptor, two TRAPP‐interactive signaling proteins, sensitizing cells to stress‐induced apoptosis. Synopsis The TRAnsport Protein Particle (TRAPP) complex, which controls multiple membrane trafficking steps along the secretory pathway, mediates cellular adaptation to acute stress by associating with and driving the recruitment of the COPII coat to stress granules (SGs), thereby halting secretion and possibly limiting energy consumption. The TRAPP complex associates with and drives the recruitment of the COPII coat to SGs.The TRAPP complex promotes the maturation of SGs.Relocation of TRAPP complex and COPII to SGs depends on CDK1/2 and occurs only in cycling cells.Association of TRAPP complex and COPII with SGs halts secretion. Graphical Abstract TRAPP‐dependent stress granule recruitment of COPII vesicle coats to halt secretion and limit energy consumption is involved in cellular adapation to acute stress. © The Author(s) 2019 |
| abstractGer |
Abstract The TRAnsport Protein Particle (TRAPP) complex controls multiple membrane trafficking steps and is strategically positioned to mediate cell adaptation to diverse environmental conditions, including acute stress. We have identified the TRAPP complex as a component of a branch of the integrated stress response that impinges on the early secretory pathway. The TRAPP complex associates with and drives the recruitment of the COPII coat to stress granules (SGs) leading to vesiculation of the Golgi complex and arrest of ER export. The relocation of the TRAPP complex and COPII to SGs only occurs in cycling cells and is CDK1/2‐dependent, being driven by the interaction of TRAPP with hnRNPK, a CDK substrate that associates with SGs when phosphorylated. In addition, CDK1/2 inhibition impairs TRAPP complex/COPII relocation to SGs while stabilizing them at ER exit sites. Importantly, the TRAPP complex controls the maturation of SGs. SGs that assemble in TRAPP‐depleted cells are smaller and are no longer able to recruit RACK1 and Raptor, two TRAPP‐interactive signaling proteins, sensitizing cells to stress‐induced apoptosis. Synopsis The TRAnsport Protein Particle (TRAPP) complex, which controls multiple membrane trafficking steps along the secretory pathway, mediates cellular adaptation to acute stress by associating with and driving the recruitment of the COPII coat to stress granules (SGs), thereby halting secretion and possibly limiting energy consumption. The TRAPP complex associates with and drives the recruitment of the COPII coat to SGs.The TRAPP complex promotes the maturation of SGs.Relocation of TRAPP complex and COPII to SGs depends on CDK1/2 and occurs only in cycling cells.Association of TRAPP complex and COPII with SGs halts secretion. Graphical Abstract TRAPP‐dependent stress granule recruitment of COPII vesicle coats to halt secretion and limit energy consumption is involved in cellular adapation to acute stress. © The Author(s) 2019 |
| abstract_unstemmed |
Abstract The TRAnsport Protein Particle (TRAPP) complex controls multiple membrane trafficking steps and is strategically positioned to mediate cell adaptation to diverse environmental conditions, including acute stress. We have identified the TRAPP complex as a component of a branch of the integrated stress response that impinges on the early secretory pathway. The TRAPP complex associates with and drives the recruitment of the COPII coat to stress granules (SGs) leading to vesiculation of the Golgi complex and arrest of ER export. The relocation of the TRAPP complex and COPII to SGs only occurs in cycling cells and is CDK1/2‐dependent, being driven by the interaction of TRAPP with hnRNPK, a CDK substrate that associates with SGs when phosphorylated. In addition, CDK1/2 inhibition impairs TRAPP complex/COPII relocation to SGs while stabilizing them at ER exit sites. Importantly, the TRAPP complex controls the maturation of SGs. SGs that assemble in TRAPP‐depleted cells are smaller and are no longer able to recruit RACK1 and Raptor, two TRAPP‐interactive signaling proteins, sensitizing cells to stress‐induced apoptosis. Synopsis The TRAnsport Protein Particle (TRAPP) complex, which controls multiple membrane trafficking steps along the secretory pathway, mediates cellular adaptation to acute stress by associating with and driving the recruitment of the COPII coat to stress granules (SGs), thereby halting secretion and possibly limiting energy consumption. The TRAPP complex associates with and drives the recruitment of the COPII coat to SGs.The TRAPP complex promotes the maturation of SGs.Relocation of TRAPP complex and COPII to SGs depends on CDK1/2 and occurs only in cycling cells.Association of TRAPP complex and COPII with SGs halts secretion. Graphical Abstract TRAPP‐dependent stress granule recruitment of COPII vesicle coats to halt secretion and limit energy consumption is involved in cellular adapation to acute stress. © The Author(s) 2019 |
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The TRAPP complex mediates secretion arrest induced by stress granule assembly |
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Wilson, Cathal Di Tullio, Giuseppe Santoro, Michele Pucci, Piero Monti, Maria D'Amico, Davide Pisonero‐Vaquero, Sandra De Cegli, Rossella Romano, Alessia Saleem, Moin A Polishchuk, Elena Failli, Mario Giaquinto, Laura De Matteis, Maria Antonietta |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000naa a22002652 4500</leader><controlfield tag="001">SPR05801635X</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20241024065138.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">241024s2019 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.15252/embj.2019101704</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR05801635X</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)embj.2019101704-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Zappa, Francesca</subfield><subfield code="e">verfasserin</subfield><subfield code="0">(orcid)0000-0003-1263-3828</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">The TRAPP complex mediates secretion arrest induced by stress granule assembly</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2019</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© The Author(s) 2019</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract The TRAnsport Protein Particle (TRAPP) complex controls multiple membrane trafficking steps and is strategically positioned to mediate cell adaptation to diverse environmental conditions, including acute stress. We have identified the TRAPP complex as a component of a branch of the integrated stress response that impinges on the early secretory pathway. The TRAPP complex associates with and drives the recruitment of the COPII coat to stress granules (SGs) leading to vesiculation of the Golgi complex and arrest of ER export. The relocation of the TRAPP complex and COPII to SGs only occurs in cycling cells and is CDK1/2‐dependent, being driven by the interaction of TRAPP with hnRNPK, a CDK substrate that associates with SGs when phosphorylated. In addition, CDK1/2 inhibition impairs TRAPP complex/COPII relocation to SGs while stabilizing them at ER exit sites. Importantly, the TRAPP complex controls the maturation of SGs. SGs that assemble in TRAPP‐depleted cells are smaller and are no longer able to recruit RACK1 and Raptor, two TRAPP‐interactive signaling proteins, sensitizing cells to stress‐induced apoptosis.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Synopsis The TRAnsport Protein Particle (TRAPP) complex, which controls multiple membrane trafficking steps along the secretory pathway, mediates cellular adaptation to acute stress by associating with and driving the recruitment of the COPII coat to stress granules (SGs), thereby halting secretion and possibly limiting energy consumption. The TRAPP complex associates with and drives the recruitment of the COPII coat to SGs.The TRAPP complex promotes the maturation of SGs.Relocation of TRAPP complex and COPII to SGs depends on CDK1/2 and occurs only in cycling cells.Association of TRAPP complex and COPII with SGs halts secretion.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Graphical Abstract TRAPP‐dependent stress granule recruitment of COPII vesicle coats to halt secretion and limit energy consumption is involved in cellular adapation to acute stress.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cdk</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">COPII</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">integrated stress response</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">stress granules</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">TRAPP complex</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wilson, Cathal</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Di Tullio, Giuseppe</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Santoro, Michele</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Pucci, Piero</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Monti, Maria</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">D'Amico, Davide</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Pisonero‐Vaquero, Sandra</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">De Cegli, Rossella</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Romano, Alessia</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Saleem, Moin A</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Polishchuk, Elena</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Failli, Mario</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Giaquinto, Laura</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">De Matteis, Maria Antonietta</subfield><subfield code="e">verfasserin</subfield><subfield code="0">(orcid)0000-0003-0053-3061</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">The EMBO Journal</subfield><subfield code="d">Nature Publishing Group UK, 2023</subfield><subfield code="g">38(2019), 19 vom: 20. 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