RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils
Abstract The aggresome is an organelle that recruits aggregated proteins for storage and degradation. We performed an siRNA screen for proteins involved in aggresome formation and identified novel mammalian AAA+ protein disaggregases RuvbL1 and RuvbL2. Depletion of RuvbL1 or RuvbL2 suppressed aggres...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Zaarur, Nava [verfasserIn] Xu, Xiaobin [verfasserIn] Lestienne, Patrick [verfasserIn] Meriin, Anatoli B [verfasserIn] McComb, Mark [verfasserIn] Costello, Catherine E [verfasserIn] Newnam, Gary P [verfasserIn] Ganti, Rakhee [verfasserIn] Romanova, Nina V [verfasserIn] Shanmugasundaram, Maruda [verfasserIn] Silva, Sara TN [verfasserIn] Bandeiras, Tiago M [verfasserIn] Matias, Pedro M [verfasserIn] Lobachev, Kirill S [verfasserIn] Lednev, Igor K [verfasserIn] Chernoff, Yury O [verfasserIn] Sherman, Michael Y [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Schlagwörter: |
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| Anmerkung: |
© The Author(s) 2015 |
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| Übergeordnetes Werk: |
Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 34(2015), 18 vom: 24. Aug., Seite 2363-2382 |
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| Übergeordnetes Werk: |
volume:34 ; year:2015 ; number:18 ; day:24 ; month:08 ; pages:2363-2382 |
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| DOI / URN: |
10.15252/embj.201591245 |
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| Katalog-ID: |
SPR058063285 |
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| 041 | |a eng | ||
| 100 | 1 | |a Zaarur, Nava |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils |
| 264 | 1 | |c 2015 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a Computermedien |b c |2 rdamedia | ||
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| 500 | |a © The Author(s) 2015 | ||
| 520 | |a Abstract The aggresome is an organelle that recruits aggregated proteins for storage and degradation. We performed an siRNA screen for proteins involved in aggresome formation and identified novel mammalian AAA+ protein disaggregases RuvbL1 and RuvbL2. Depletion of RuvbL1 or RuvbL2 suppressed aggresome formation and caused buildup of multiple cytoplasmic aggregates. Similarly, downregulation of RuvbL orthologs in yeast suppressed the formation of an aggresome‐like body and enhanced the aggregate toxicity. In contrast, their overproduction enhanced the resistance to proteotoxic stress independently of chaperone Hsp104. Mammalian RuvbL associated with the aggresome, and the aggresome substrate synphilin‐1 interacted directly with the RuvbL1 barrel‐like structure near the opening of the central channel. Importantly, polypeptides with unfolded structures and amyloid fibrils stimulated the ATPase activity of RuvbL. Finally, disassembly of protein aggregates was promoted by RuvbL. These data indicate that RuvbL complexes serve as chaperones in protein disaggregation. | ||
| 520 | |a Synopsis The AAA+ ATPase RuvbL is required for aggresome formation and serves as a protein disaggregase that can disassemble amyloids in mammalian and yeast cells. Depletion of AAA+ ATPases RuvbL1 or RuvbL2 enhances aggregation of certain proteins in mammalian cells and inhibits aggresome formation.RuvbL directly interacts with aggresome substrates, and the site of interaction is in the proximity to the internal channel of its barrel‐like structure.Purified RuvbL inhibits seeding and promotes fragmentation of amyloid fibrils.RuvbL depletion slows down disassembly of protein aggregates in mammalian cells and enhances proteotoxicity.In yeast, RuvbL orthologs protect from heat shock and protein toxicity independently of Hsp104. | ||
| 520 | |a Graphical Abstract The AAA+ ATPase RuvbL is required for aggresome formation and serves as a protein disaggregase that can disassemble amyloids in mammalian and yeast cells. | ||
| 650 | 4 | |a aggresome |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a amyloid |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a disaggregation |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a RuvbL |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Xu, Xiaobin |e verfasserin |4 aut | |
| 700 | 1 | |a Lestienne, Patrick |e verfasserin |4 aut | |
| 700 | 1 | |a Meriin, Anatoli B |e verfasserin |4 aut | |
| 700 | 1 | |a McComb, Mark |e verfasserin |4 aut | |
| 700 | 1 | |a Costello, Catherine E |e verfasserin |4 aut | |
| 700 | 1 | |a Newnam, Gary P |e verfasserin |4 aut | |
| 700 | 1 | |a Ganti, Rakhee |e verfasserin |4 aut | |
| 700 | 1 | |a Romanova, Nina V |e verfasserin |4 aut | |
| 700 | 1 | |a Shanmugasundaram, Maruda |e verfasserin |4 aut | |
| 700 | 1 | |a Silva, Sara TN |e verfasserin |4 aut | |
| 700 | 1 | |a Bandeiras, Tiago M |e verfasserin |4 aut | |
| 700 | 1 | |a Matias, Pedro M |e verfasserin |4 aut | |
| 700 | 1 | |a Lobachev, Kirill S |e verfasserin |4 aut | |
| 700 | 1 | |a Lednev, Igor K |e verfasserin |4 aut | |
| 700 | 1 | |a Chernoff, Yury O |e verfasserin |4 aut | |
| 700 | 1 | |a Sherman, Michael Y |e verfasserin |4 aut | |
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10.15252/embj.201591245 doi (DE-627)SPR058063285 (SPR)embj.201591245-e DE-627 ger DE-627 rakwb eng Zaarur, Nava verfasserin aut RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2015 Abstract The aggresome is an organelle that recruits aggregated proteins for storage and degradation. We performed an siRNA screen for proteins involved in aggresome formation and identified novel mammalian AAA+ protein disaggregases RuvbL1 and RuvbL2. Depletion of RuvbL1 or RuvbL2 suppressed aggresome formation and caused buildup of multiple cytoplasmic aggregates. Similarly, downregulation of RuvbL orthologs in yeast suppressed the formation of an aggresome‐like body and enhanced the aggregate toxicity. In contrast, their overproduction enhanced the resistance to proteotoxic stress independently of chaperone Hsp104. Mammalian RuvbL associated with the aggresome, and the aggresome substrate synphilin‐1 interacted directly with the RuvbL1 barrel‐like structure near the opening of the central channel. Importantly, polypeptides with unfolded structures and amyloid fibrils stimulated the ATPase activity of RuvbL. Finally, disassembly of protein aggregates was promoted by RuvbL. These data indicate that RuvbL complexes serve as chaperones in protein disaggregation. Synopsis The AAA+ ATPase RuvbL is required for aggresome formation and serves as a protein disaggregase that can disassemble amyloids in mammalian and yeast cells. Depletion of AAA+ ATPases RuvbL1 or RuvbL2 enhances aggregation of certain proteins in mammalian cells and inhibits aggresome formation.RuvbL directly interacts with aggresome substrates, and the site of interaction is in the proximity to the internal channel of its barrel‐like structure.Purified RuvbL inhibits seeding and promotes fragmentation of amyloid fibrils.RuvbL depletion slows down disassembly of protein aggregates in mammalian cells and enhances proteotoxicity.In yeast, RuvbL orthologs protect from heat shock and protein toxicity independently of Hsp104. Graphical Abstract The AAA+ ATPase RuvbL is required for aggresome formation and serves as a protein disaggregase that can disassemble amyloids in mammalian and yeast cells. aggresome (dpeaa)DE-He213 amyloid (dpeaa)DE-He213 disaggregation (dpeaa)DE-He213 RuvbL (dpeaa)DE-He213 Xu, Xiaobin verfasserin aut Lestienne, Patrick verfasserin aut Meriin, Anatoli B verfasserin aut McComb, Mark verfasserin aut Costello, Catherine E verfasserin aut Newnam, Gary P verfasserin aut Ganti, Rakhee verfasserin aut Romanova, Nina V verfasserin aut Shanmugasundaram, Maruda verfasserin aut Silva, Sara TN verfasserin aut Bandeiras, Tiago M verfasserin aut Matias, Pedro M verfasserin aut Lobachev, Kirill S verfasserin aut Lednev, Igor K verfasserin aut Chernoff, Yury O verfasserin aut Sherman, Michael Y verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 34(2015), 18 vom: 24. Aug., Seite 2363-2382 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:34 year:2015 number:18 day:24 month:08 pages:2363-2382 https://dx.doi.org/10.15252/embj.201591245 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_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_2018 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_2188 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 34 2015 18 24 08 2363-2382 |
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10.15252/embj.201591245 doi (DE-627)SPR058063285 (SPR)embj.201591245-e DE-627 ger DE-627 rakwb eng Zaarur, Nava verfasserin aut RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2015 Abstract The aggresome is an organelle that recruits aggregated proteins for storage and degradation. We performed an siRNA screen for proteins involved in aggresome formation and identified novel mammalian AAA+ protein disaggregases RuvbL1 and RuvbL2. Depletion of RuvbL1 or RuvbL2 suppressed aggresome formation and caused buildup of multiple cytoplasmic aggregates. Similarly, downregulation of RuvbL orthologs in yeast suppressed the formation of an aggresome‐like body and enhanced the aggregate toxicity. In contrast, their overproduction enhanced the resistance to proteotoxic stress independently of chaperone Hsp104. Mammalian RuvbL associated with the aggresome, and the aggresome substrate synphilin‐1 interacted directly with the RuvbL1 barrel‐like structure near the opening of the central channel. Importantly, polypeptides with unfolded structures and amyloid fibrils stimulated the ATPase activity of RuvbL. Finally, disassembly of protein aggregates was promoted by RuvbL. These data indicate that RuvbL complexes serve as chaperones in protein disaggregation. Synopsis The AAA+ ATPase RuvbL is required for aggresome formation and serves as a protein disaggregase that can disassemble amyloids in mammalian and yeast cells. Depletion of AAA+ ATPases RuvbL1 or RuvbL2 enhances aggregation of certain proteins in mammalian cells and inhibits aggresome formation.RuvbL directly interacts with aggresome substrates, and the site of interaction is in the proximity to the internal channel of its barrel‐like structure.Purified RuvbL inhibits seeding and promotes fragmentation of amyloid fibrils.RuvbL depletion slows down disassembly of protein aggregates in mammalian cells and enhances proteotoxicity.In yeast, RuvbL orthologs protect from heat shock and protein toxicity independently of Hsp104. Graphical Abstract The AAA+ ATPase RuvbL is required for aggresome formation and serves as a protein disaggregase that can disassemble amyloids in mammalian and yeast cells. aggresome (dpeaa)DE-He213 amyloid (dpeaa)DE-He213 disaggregation (dpeaa)DE-He213 RuvbL (dpeaa)DE-He213 Xu, Xiaobin verfasserin aut Lestienne, Patrick verfasserin aut Meriin, Anatoli B verfasserin aut McComb, Mark verfasserin aut Costello, Catherine E verfasserin aut Newnam, Gary P verfasserin aut Ganti, Rakhee verfasserin aut Romanova, Nina V verfasserin aut Shanmugasundaram, Maruda verfasserin aut Silva, Sara TN verfasserin aut Bandeiras, Tiago M verfasserin aut Matias, Pedro M verfasserin aut Lobachev, Kirill S verfasserin aut Lednev, Igor K verfasserin aut Chernoff, Yury O verfasserin aut Sherman, Michael Y verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 34(2015), 18 vom: 24. Aug., Seite 2363-2382 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:34 year:2015 number:18 day:24 month:08 pages:2363-2382 https://dx.doi.org/10.15252/embj.201591245 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_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_2018 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_2188 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 34 2015 18 24 08 2363-2382 |
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10.15252/embj.201591245 doi (DE-627)SPR058063285 (SPR)embj.201591245-e DE-627 ger DE-627 rakwb eng Zaarur, Nava verfasserin aut RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2015 Abstract The aggresome is an organelle that recruits aggregated proteins for storage and degradation. We performed an siRNA screen for proteins involved in aggresome formation and identified novel mammalian AAA+ protein disaggregases RuvbL1 and RuvbL2. Depletion of RuvbL1 or RuvbL2 suppressed aggresome formation and caused buildup of multiple cytoplasmic aggregates. Similarly, downregulation of RuvbL orthologs in yeast suppressed the formation of an aggresome‐like body and enhanced the aggregate toxicity. In contrast, their overproduction enhanced the resistance to proteotoxic stress independently of chaperone Hsp104. Mammalian RuvbL associated with the aggresome, and the aggresome substrate synphilin‐1 interacted directly with the RuvbL1 barrel‐like structure near the opening of the central channel. Importantly, polypeptides with unfolded structures and amyloid fibrils stimulated the ATPase activity of RuvbL. Finally, disassembly of protein aggregates was promoted by RuvbL. These data indicate that RuvbL complexes serve as chaperones in protein disaggregation. Synopsis The AAA+ ATPase RuvbL is required for aggresome formation and serves as a protein disaggregase that can disassemble amyloids in mammalian and yeast cells. Depletion of AAA+ ATPases RuvbL1 or RuvbL2 enhances aggregation of certain proteins in mammalian cells and inhibits aggresome formation.RuvbL directly interacts with aggresome substrates, and the site of interaction is in the proximity to the internal channel of its barrel‐like structure.Purified RuvbL inhibits seeding and promotes fragmentation of amyloid fibrils.RuvbL depletion slows down disassembly of protein aggregates in mammalian cells and enhances proteotoxicity.In yeast, RuvbL orthologs protect from heat shock and protein toxicity independently of Hsp104. Graphical Abstract The AAA+ ATPase RuvbL is required for aggresome formation and serves as a protein disaggregase that can disassemble amyloids in mammalian and yeast cells. aggresome (dpeaa)DE-He213 amyloid (dpeaa)DE-He213 disaggregation (dpeaa)DE-He213 RuvbL (dpeaa)DE-He213 Xu, Xiaobin verfasserin aut Lestienne, Patrick verfasserin aut Meriin, Anatoli B verfasserin aut McComb, Mark verfasserin aut Costello, Catherine E verfasserin aut Newnam, Gary P verfasserin aut Ganti, Rakhee verfasserin aut Romanova, Nina V verfasserin aut Shanmugasundaram, Maruda verfasserin aut Silva, Sara TN verfasserin aut Bandeiras, Tiago M verfasserin aut Matias, Pedro M verfasserin aut Lobachev, Kirill S verfasserin aut Lednev, Igor K verfasserin aut Chernoff, Yury O verfasserin aut Sherman, Michael Y verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 34(2015), 18 vom: 24. Aug., Seite 2363-2382 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:34 year:2015 number:18 day:24 month:08 pages:2363-2382 https://dx.doi.org/10.15252/embj.201591245 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_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_2018 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_2188 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 34 2015 18 24 08 2363-2382 |
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10.15252/embj.201591245 doi (DE-627)SPR058063285 (SPR)embj.201591245-e DE-627 ger DE-627 rakwb eng Zaarur, Nava verfasserin aut RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2015 Abstract The aggresome is an organelle that recruits aggregated proteins for storage and degradation. We performed an siRNA screen for proteins involved in aggresome formation and identified novel mammalian AAA+ protein disaggregases RuvbL1 and RuvbL2. Depletion of RuvbL1 or RuvbL2 suppressed aggresome formation and caused buildup of multiple cytoplasmic aggregates. Similarly, downregulation of RuvbL orthologs in yeast suppressed the formation of an aggresome‐like body and enhanced the aggregate toxicity. In contrast, their overproduction enhanced the resistance to proteotoxic stress independently of chaperone Hsp104. Mammalian RuvbL associated with the aggresome, and the aggresome substrate synphilin‐1 interacted directly with the RuvbL1 barrel‐like structure near the opening of the central channel. Importantly, polypeptides with unfolded structures and amyloid fibrils stimulated the ATPase activity of RuvbL. Finally, disassembly of protein aggregates was promoted by RuvbL. These data indicate that RuvbL complexes serve as chaperones in protein disaggregation. Synopsis The AAA+ ATPase RuvbL is required for aggresome formation and serves as a protein disaggregase that can disassemble amyloids in mammalian and yeast cells. Depletion of AAA+ ATPases RuvbL1 or RuvbL2 enhances aggregation of certain proteins in mammalian cells and inhibits aggresome formation.RuvbL directly interacts with aggresome substrates, and the site of interaction is in the proximity to the internal channel of its barrel‐like structure.Purified RuvbL inhibits seeding and promotes fragmentation of amyloid fibrils.RuvbL depletion slows down disassembly of protein aggregates in mammalian cells and enhances proteotoxicity.In yeast, RuvbL orthologs protect from heat shock and protein toxicity independently of Hsp104. Graphical Abstract The AAA+ ATPase RuvbL is required for aggresome formation and serves as a protein disaggregase that can disassemble amyloids in mammalian and yeast cells. aggresome (dpeaa)DE-He213 amyloid (dpeaa)DE-He213 disaggregation (dpeaa)DE-He213 RuvbL (dpeaa)DE-He213 Xu, Xiaobin verfasserin aut Lestienne, Patrick verfasserin aut Meriin, Anatoli B verfasserin aut McComb, Mark verfasserin aut Costello, Catherine E verfasserin aut Newnam, Gary P verfasserin aut Ganti, Rakhee verfasserin aut Romanova, Nina V verfasserin aut Shanmugasundaram, Maruda verfasserin aut Silva, Sara TN verfasserin aut Bandeiras, Tiago M verfasserin aut Matias, Pedro M verfasserin aut Lobachev, Kirill S verfasserin aut Lednev, Igor K verfasserin aut Chernoff, Yury O verfasserin aut Sherman, Michael Y verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 34(2015), 18 vom: 24. Aug., Seite 2363-2382 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:34 year:2015 number:18 day:24 month:08 pages:2363-2382 https://dx.doi.org/10.15252/embj.201591245 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_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_2018 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_2188 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 34 2015 18 24 08 2363-2382 |
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10.15252/embj.201591245 doi (DE-627)SPR058063285 (SPR)embj.201591245-e DE-627 ger DE-627 rakwb eng Zaarur, Nava verfasserin aut RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2015 Abstract The aggresome is an organelle that recruits aggregated proteins for storage and degradation. We performed an siRNA screen for proteins involved in aggresome formation and identified novel mammalian AAA+ protein disaggregases RuvbL1 and RuvbL2. Depletion of RuvbL1 or RuvbL2 suppressed aggresome formation and caused buildup of multiple cytoplasmic aggregates. Similarly, downregulation of RuvbL orthologs in yeast suppressed the formation of an aggresome‐like body and enhanced the aggregate toxicity. In contrast, their overproduction enhanced the resistance to proteotoxic stress independently of chaperone Hsp104. Mammalian RuvbL associated with the aggresome, and the aggresome substrate synphilin‐1 interacted directly with the RuvbL1 barrel‐like structure near the opening of the central channel. Importantly, polypeptides with unfolded structures and amyloid fibrils stimulated the ATPase activity of RuvbL. Finally, disassembly of protein aggregates was promoted by RuvbL. These data indicate that RuvbL complexes serve as chaperones in protein disaggregation. Synopsis The AAA+ ATPase RuvbL is required for aggresome formation and serves as a protein disaggregase that can disassemble amyloids in mammalian and yeast cells. Depletion of AAA+ ATPases RuvbL1 or RuvbL2 enhances aggregation of certain proteins in mammalian cells and inhibits aggresome formation.RuvbL directly interacts with aggresome substrates, and the site of interaction is in the proximity to the internal channel of its barrel‐like structure.Purified RuvbL inhibits seeding and promotes fragmentation of amyloid fibrils.RuvbL depletion slows down disassembly of protein aggregates in mammalian cells and enhances proteotoxicity.In yeast, RuvbL orthologs protect from heat shock and protein toxicity independently of Hsp104. Graphical Abstract The AAA+ ATPase RuvbL is required for aggresome formation and serves as a protein disaggregase that can disassemble amyloids in mammalian and yeast cells. aggresome (dpeaa)DE-He213 amyloid (dpeaa)DE-He213 disaggregation (dpeaa)DE-He213 RuvbL (dpeaa)DE-He213 Xu, Xiaobin verfasserin aut Lestienne, Patrick verfasserin aut Meriin, Anatoli B verfasserin aut McComb, Mark verfasserin aut Costello, Catherine E verfasserin aut Newnam, Gary P verfasserin aut Ganti, Rakhee verfasserin aut Romanova, Nina V verfasserin aut Shanmugasundaram, Maruda verfasserin aut Silva, Sara TN verfasserin aut Bandeiras, Tiago M verfasserin aut Matias, Pedro M verfasserin aut Lobachev, Kirill S verfasserin aut Lednev, Igor K verfasserin aut Chernoff, Yury O verfasserin aut Sherman, Michael Y verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 34(2015), 18 vom: 24. Aug., Seite 2363-2382 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:34 year:2015 number:18 day:24 month:08 pages:2363-2382 https://dx.doi.org/10.15252/embj.201591245 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_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_2018 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_2188 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 34 2015 18 24 08 2363-2382 |
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Enthalten in The EMBO Journal 34(2015), 18 vom: 24. Aug., Seite 2363-2382 volume:34 year:2015 number:18 day:24 month:08 pages:2363-2382 |
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Enthalten in The EMBO Journal 34(2015), 18 vom: 24. Aug., Seite 2363-2382 volume:34 year:2015 number:18 day:24 month:08 pages:2363-2382 |
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aggresome amyloid disaggregation RuvbL |
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Zaarur, Nava @@aut@@ Xu, Xiaobin @@aut@@ Lestienne, Patrick @@aut@@ Meriin, Anatoli B @@aut@@ McComb, Mark @@aut@@ Costello, Catherine E @@aut@@ Newnam, Gary P @@aut@@ Ganti, Rakhee @@aut@@ Romanova, Nina V @@aut@@ Shanmugasundaram, Maruda @@aut@@ Silva, Sara TN @@aut@@ Bandeiras, Tiago M @@aut@@ Matias, Pedro M @@aut@@ Lobachev, Kirill S @@aut@@ Lednev, Igor K @@aut@@ Chernoff, Yury O @@aut@@ Sherman, Michael Y @@aut@@ |
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2015-08-24T00:00:00Z |
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englisch |
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|
| author |
Zaarur, Nava |
| spellingShingle |
Zaarur, Nava misc aggresome misc amyloid misc disaggregation misc RuvbL RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils |
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1460-2075 |
| topic_title |
RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils aggresome (dpeaa)DE-He213 amyloid (dpeaa)DE-He213 disaggregation (dpeaa)DE-He213 RuvbL (dpeaa)DE-He213 |
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misc aggresome misc amyloid misc disaggregation misc RuvbL |
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misc aggresome misc amyloid misc disaggregation misc RuvbL |
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misc aggresome misc amyloid misc disaggregation misc RuvbL |
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Elektronische Aufsätze Aufsätze Elektronische Ressource |
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The EMBO Journal |
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The EMBO Journal |
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RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils |
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(DE-627)SPR058063285 (SPR)embj.201591245-e |
| title_full |
RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils |
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Zaarur, Nava |
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The EMBO Journal |
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The EMBO Journal |
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Zaarur, Nava Xu, Xiaobin Lestienne, Patrick Meriin, Anatoli B McComb, Mark Costello, Catherine E Newnam, Gary P Ganti, Rakhee Romanova, Nina V Shanmugasundaram, Maruda Silva, Sara TN Bandeiras, Tiago M Matias, Pedro M Lobachev, Kirill S Lednev, Igor K Chernoff, Yury O Sherman, Michael Y |
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34 |
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Elektronische Aufsätze |
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Zaarur, Nava |
| doi_str_mv |
10.15252/embj.201591245 |
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verfasserin |
| title_sort |
ruvbl1 and ruvbl2 enhance aggresome formation and disaggregate amyloid fibrils |
| title_auth |
RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils |
| abstract |
Abstract The aggresome is an organelle that recruits aggregated proteins for storage and degradation. We performed an siRNA screen for proteins involved in aggresome formation and identified novel mammalian AAA+ protein disaggregases RuvbL1 and RuvbL2. Depletion of RuvbL1 or RuvbL2 suppressed aggresome formation and caused buildup of multiple cytoplasmic aggregates. Similarly, downregulation of RuvbL orthologs in yeast suppressed the formation of an aggresome‐like body and enhanced the aggregate toxicity. In contrast, their overproduction enhanced the resistance to proteotoxic stress independently of chaperone Hsp104. Mammalian RuvbL associated with the aggresome, and the aggresome substrate synphilin‐1 interacted directly with the RuvbL1 barrel‐like structure near the opening of the central channel. Importantly, polypeptides with unfolded structures and amyloid fibrils stimulated the ATPase activity of RuvbL. Finally, disassembly of protein aggregates was promoted by RuvbL. These data indicate that RuvbL complexes serve as chaperones in protein disaggregation. Synopsis The AAA+ ATPase RuvbL is required for aggresome formation and serves as a protein disaggregase that can disassemble amyloids in mammalian and yeast cells. Depletion of AAA+ ATPases RuvbL1 or RuvbL2 enhances aggregation of certain proteins in mammalian cells and inhibits aggresome formation.RuvbL directly interacts with aggresome substrates, and the site of interaction is in the proximity to the internal channel of its barrel‐like structure.Purified RuvbL inhibits seeding and promotes fragmentation of amyloid fibrils.RuvbL depletion slows down disassembly of protein aggregates in mammalian cells and enhances proteotoxicity.In yeast, RuvbL orthologs protect from heat shock and protein toxicity independently of Hsp104. Graphical Abstract The AAA+ ATPase RuvbL is required for aggresome formation and serves as a protein disaggregase that can disassemble amyloids in mammalian and yeast cells. © The Author(s) 2015 |
| abstractGer |
Abstract The aggresome is an organelle that recruits aggregated proteins for storage and degradation. We performed an siRNA screen for proteins involved in aggresome formation and identified novel mammalian AAA+ protein disaggregases RuvbL1 and RuvbL2. Depletion of RuvbL1 or RuvbL2 suppressed aggresome formation and caused buildup of multiple cytoplasmic aggregates. Similarly, downregulation of RuvbL orthologs in yeast suppressed the formation of an aggresome‐like body and enhanced the aggregate toxicity. In contrast, their overproduction enhanced the resistance to proteotoxic stress independently of chaperone Hsp104. Mammalian RuvbL associated with the aggresome, and the aggresome substrate synphilin‐1 interacted directly with the RuvbL1 barrel‐like structure near the opening of the central channel. Importantly, polypeptides with unfolded structures and amyloid fibrils stimulated the ATPase activity of RuvbL. Finally, disassembly of protein aggregates was promoted by RuvbL. These data indicate that RuvbL complexes serve as chaperones in protein disaggregation. Synopsis The AAA+ ATPase RuvbL is required for aggresome formation and serves as a protein disaggregase that can disassemble amyloids in mammalian and yeast cells. Depletion of AAA+ ATPases RuvbL1 or RuvbL2 enhances aggregation of certain proteins in mammalian cells and inhibits aggresome formation.RuvbL directly interacts with aggresome substrates, and the site of interaction is in the proximity to the internal channel of its barrel‐like structure.Purified RuvbL inhibits seeding and promotes fragmentation of amyloid fibrils.RuvbL depletion slows down disassembly of protein aggregates in mammalian cells and enhances proteotoxicity.In yeast, RuvbL orthologs protect from heat shock and protein toxicity independently of Hsp104. Graphical Abstract The AAA+ ATPase RuvbL is required for aggresome formation and serves as a protein disaggregase that can disassemble amyloids in mammalian and yeast cells. © The Author(s) 2015 |
| abstract_unstemmed |
Abstract The aggresome is an organelle that recruits aggregated proteins for storage and degradation. We performed an siRNA screen for proteins involved in aggresome formation and identified novel mammalian AAA+ protein disaggregases RuvbL1 and RuvbL2. Depletion of RuvbL1 or RuvbL2 suppressed aggresome formation and caused buildup of multiple cytoplasmic aggregates. Similarly, downregulation of RuvbL orthologs in yeast suppressed the formation of an aggresome‐like body and enhanced the aggregate toxicity. In contrast, their overproduction enhanced the resistance to proteotoxic stress independently of chaperone Hsp104. Mammalian RuvbL associated with the aggresome, and the aggresome substrate synphilin‐1 interacted directly with the RuvbL1 barrel‐like structure near the opening of the central channel. Importantly, polypeptides with unfolded structures and amyloid fibrils stimulated the ATPase activity of RuvbL. Finally, disassembly of protein aggregates was promoted by RuvbL. These data indicate that RuvbL complexes serve as chaperones in protein disaggregation. Synopsis The AAA+ ATPase RuvbL is required for aggresome formation and serves as a protein disaggregase that can disassemble amyloids in mammalian and yeast cells. Depletion of AAA+ ATPases RuvbL1 or RuvbL2 enhances aggregation of certain proteins in mammalian cells and inhibits aggresome formation.RuvbL directly interacts with aggresome substrates, and the site of interaction is in the proximity to the internal channel of its barrel‐like structure.Purified RuvbL inhibits seeding and promotes fragmentation of amyloid fibrils.RuvbL depletion slows down disassembly of protein aggregates in mammalian cells and enhances proteotoxicity.In yeast, RuvbL orthologs protect from heat shock and protein toxicity independently of Hsp104. Graphical Abstract The AAA+ ATPase RuvbL is required for aggresome formation and serves as a protein disaggregase that can disassemble amyloids in mammalian and yeast cells. © The Author(s) 2015 |
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RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils |
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https://dx.doi.org/10.15252/embj.201591245 |
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Xu, Xiaobin Lestienne, Patrick Meriin, Anatoli B McComb, Mark Costello, Catherine E Newnam, Gary P Ganti, Rakhee Romanova, Nina V Shanmugasundaram, Maruda Silva, Sara TN Bandeiras, Tiago M Matias, Pedro M Lobachev, Kirill S Lednev, Igor K Chernoff, Yury O Sherman, Michael Y |
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Xu, Xiaobin Lestienne, Patrick Meriin, Anatoli B McComb, Mark Costello, Catherine E Newnam, Gary P Ganti, Rakhee Romanova, Nina V Shanmugasundaram, Maruda Silva, Sara TN Bandeiras, Tiago M Matias, Pedro M Lobachev, Kirill S Lednev, Igor K Chernoff, Yury O Sherman, Michael Y |
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10.15252/embj.201591245 |
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2024-10-25T04:56:38.835Z |
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| score |
7.4016933 |