Mutually Exclusive CBC-Containing Complexes Contribute to RNA Fate

The nuclear cap-binding complex (CBC) stimulates processing reactions of capped RNAs, including their splicing, 3′-end formation, degradation, and transport. CBC effects are particular for individual RNA families, but how such selectivity is achieved remains elusive. Here, we analyze three main CBC...
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Autor*in:	Simone Giacometti [verfasserIn] Nour El Houda Benbahouche [verfasserIn] Michal Domanski [verfasserIn] Marie-Cécile Robert [verfasserIn] Nicola Meola [verfasserIn] Michal Lubas [verfasserIn] Jakob Bukenborg [verfasserIn] Jens S. Andersen [verfasserIn] Wiebke M. Schulze [verfasserIn] Celine Verheggen [verfasserIn] Grzegorz Kudla [verfasserIn] Torben Heick Jensen [verfasserIn] Edouard Bertrand [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2017

Schlagwörter:	RNA fate decisions RNA decay RNA transport cap RNA cap CLIP CBC CBC interacting proteins FRAP

Übergeordnetes Werk:	In: Cell Reports - Elsevier, 2015, 18(2017), 11, Seite 2635-2650
Übergeordnetes Werk:	volume:18 ; year:2017 ; number:11 ; pages:2635-2650

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1016/j.celrep.2017.02.046

Katalog-ID:	DOAJ021058598

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520			\|a The nuclear cap-binding complex (CBC) stimulates processing reactions of capped RNAs, including their splicing, 3′-end formation, degradation, and transport. CBC effects are particular for individual RNA families, but how such selectivity is achieved remains elusive. Here, we analyze three main CBC partners known to impact different RNA species. ARS2 stimulates 3′-end formation/transcription termination of several transcript types, ZC3H18 stimulates degradation of a diverse set of RNAs, and PHAX functions in pre-small nuclear RNA/small nucleolar RNA (pre-snRNA/snoRNA) transport. Surprisingly, these proteins all bind capped RNAs without strong preferences for given transcripts, and their steady-state binding correlates poorly with their function. Despite this, PHAX and ZC3H18 compete for CBC binding and we demonstrate that this competitive binding is functionally relevant. We further show that CBC-containing complexes are short lived in vivo, and we therefore suggest that RNA fate involves the transient formation of mutually exclusive CBC complexes, which may only be consequential at particular checkpoints during RNA biogenesis.
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700	0		\|a Celine Verheggen \|e verfasserin \|4 aut
700	0		\|a Grzegorz Kudla \|e verfasserin \|4 aut
700	0		\|a Torben Heick Jensen \|e verfasserin \|4 aut
700	0		\|a Edouard Bertrand \|e verfasserin \|4 aut
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allfields	10.1016/j.celrep.2017.02.046 doi (DE-627)DOAJ021058598 (DE-599)DOAJ173fd29c006e48f3b1da6b440058ecb1 DE-627 ger DE-627 rakwb eng QH301-705.5 Simone Giacometti verfasserin aut Mutually Exclusive CBC-Containing Complexes Contribute to RNA Fate 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The nuclear cap-binding complex (CBC) stimulates processing reactions of capped RNAs, including their splicing, 3′-end formation, degradation, and transport. CBC effects are particular for individual RNA families, but how such selectivity is achieved remains elusive. Here, we analyze three main CBC partners known to impact different RNA species. ARS2 stimulates 3′-end formation/transcription termination of several transcript types, ZC3H18 stimulates degradation of a diverse set of RNAs, and PHAX functions in pre-small nuclear RNA/small nucleolar RNA (pre-snRNA/snoRNA) transport. Surprisingly, these proteins all bind capped RNAs without strong preferences for given transcripts, and their steady-state binding correlates poorly with their function. Despite this, PHAX and ZC3H18 compete for CBC binding and we demonstrate that this competitive binding is functionally relevant. We further show that CBC-containing complexes are short lived in vivo, and we therefore suggest that RNA fate involves the transient formation of mutually exclusive CBC complexes, which may only be consequential at particular checkpoints during RNA biogenesis. RNA fate decisions RNA decay RNA transport cap RNA cap CLIP CBC CBC interacting proteins FRAP Biology (General) Nour El Houda Benbahouche verfasserin aut Michal Domanski verfasserin aut Marie-Cécile Robert verfasserin aut Nicola Meola verfasserin aut Michal Lubas verfasserin aut Jakob Bukenborg verfasserin aut Jens S. Andersen verfasserin aut Wiebke M. Schulze verfasserin aut Celine Verheggen verfasserin aut Grzegorz Kudla verfasserin aut Torben Heick Jensen verfasserin aut Edouard Bertrand verfasserin aut In Cell Reports Elsevier, 2015 18(2017), 11, Seite 2635-2650 (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:18 year:2017 number:11 pages:2635-2650 https://doi.org/10.1016/j.celrep.2017.02.046 kostenfrei https://doaj.org/article/173fd29c006e48f3b1da6b440058ecb1 kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124717302449 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 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_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 18 2017 11 2635-2650
spelling	10.1016/j.celrep.2017.02.046 doi (DE-627)DOAJ021058598 (DE-599)DOAJ173fd29c006e48f3b1da6b440058ecb1 DE-627 ger DE-627 rakwb eng QH301-705.5 Simone Giacometti verfasserin aut Mutually Exclusive CBC-Containing Complexes Contribute to RNA Fate 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The nuclear cap-binding complex (CBC) stimulates processing reactions of capped RNAs, including their splicing, 3′-end formation, degradation, and transport. CBC effects are particular for individual RNA families, but how such selectivity is achieved remains elusive. Here, we analyze three main CBC partners known to impact different RNA species. ARS2 stimulates 3′-end formation/transcription termination of several transcript types, ZC3H18 stimulates degradation of a diverse set of RNAs, and PHAX functions in pre-small nuclear RNA/small nucleolar RNA (pre-snRNA/snoRNA) transport. Surprisingly, these proteins all bind capped RNAs without strong preferences for given transcripts, and their steady-state binding correlates poorly with their function. Despite this, PHAX and ZC3H18 compete for CBC binding and we demonstrate that this competitive binding is functionally relevant. We further show that CBC-containing complexes are short lived in vivo, and we therefore suggest that RNA fate involves the transient formation of mutually exclusive CBC complexes, which may only be consequential at particular checkpoints during RNA biogenesis. RNA fate decisions RNA decay RNA transport cap RNA cap CLIP CBC CBC interacting proteins FRAP Biology (General) Nour El Houda Benbahouche verfasserin aut Michal Domanski verfasserin aut Marie-Cécile Robert verfasserin aut Nicola Meola verfasserin aut Michal Lubas verfasserin aut Jakob Bukenborg verfasserin aut Jens S. Andersen verfasserin aut Wiebke M. Schulze verfasserin aut Celine Verheggen verfasserin aut Grzegorz Kudla verfasserin aut Torben Heick Jensen verfasserin aut Edouard Bertrand verfasserin aut In Cell Reports Elsevier, 2015 18(2017), 11, Seite 2635-2650 (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:18 year:2017 number:11 pages:2635-2650 https://doi.org/10.1016/j.celrep.2017.02.046 kostenfrei https://doaj.org/article/173fd29c006e48f3b1da6b440058ecb1 kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124717302449 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 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_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 18 2017 11 2635-2650
allfields_unstemmed	10.1016/j.celrep.2017.02.046 doi (DE-627)DOAJ021058598 (DE-599)DOAJ173fd29c006e48f3b1da6b440058ecb1 DE-627 ger DE-627 rakwb eng QH301-705.5 Simone Giacometti verfasserin aut Mutually Exclusive CBC-Containing Complexes Contribute to RNA Fate 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The nuclear cap-binding complex (CBC) stimulates processing reactions of capped RNAs, including their splicing, 3′-end formation, degradation, and transport. CBC effects are particular for individual RNA families, but how such selectivity is achieved remains elusive. Here, we analyze three main CBC partners known to impact different RNA species. ARS2 stimulates 3′-end formation/transcription termination of several transcript types, ZC3H18 stimulates degradation of a diverse set of RNAs, and PHAX functions in pre-small nuclear RNA/small nucleolar RNA (pre-snRNA/snoRNA) transport. Surprisingly, these proteins all bind capped RNAs without strong preferences for given transcripts, and their steady-state binding correlates poorly with their function. Despite this, PHAX and ZC3H18 compete for CBC binding and we demonstrate that this competitive binding is functionally relevant. We further show that CBC-containing complexes are short lived in vivo, and we therefore suggest that RNA fate involves the transient formation of mutually exclusive CBC complexes, which may only be consequential at particular checkpoints during RNA biogenesis. RNA fate decisions RNA decay RNA transport cap RNA cap CLIP CBC CBC interacting proteins FRAP Biology (General) Nour El Houda Benbahouche verfasserin aut Michal Domanski verfasserin aut Marie-Cécile Robert verfasserin aut Nicola Meola verfasserin aut Michal Lubas verfasserin aut Jakob Bukenborg verfasserin aut Jens S. Andersen verfasserin aut Wiebke M. Schulze verfasserin aut Celine Verheggen verfasserin aut Grzegorz Kudla verfasserin aut Torben Heick Jensen verfasserin aut Edouard Bertrand verfasserin aut In Cell Reports Elsevier, 2015 18(2017), 11, Seite 2635-2650 (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:18 year:2017 number:11 pages:2635-2650 https://doi.org/10.1016/j.celrep.2017.02.046 kostenfrei https://doaj.org/article/173fd29c006e48f3b1da6b440058ecb1 kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124717302449 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 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_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 18 2017 11 2635-2650
allfieldsGer	10.1016/j.celrep.2017.02.046 doi (DE-627)DOAJ021058598 (DE-599)DOAJ173fd29c006e48f3b1da6b440058ecb1 DE-627 ger DE-627 rakwb eng QH301-705.5 Simone Giacometti verfasserin aut Mutually Exclusive CBC-Containing Complexes Contribute to RNA Fate 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The nuclear cap-binding complex (CBC) stimulates processing reactions of capped RNAs, including their splicing, 3′-end formation, degradation, and transport. CBC effects are particular for individual RNA families, but how such selectivity is achieved remains elusive. Here, we analyze three main CBC partners known to impact different RNA species. ARS2 stimulates 3′-end formation/transcription termination of several transcript types, ZC3H18 stimulates degradation of a diverse set of RNAs, and PHAX functions in pre-small nuclear RNA/small nucleolar RNA (pre-snRNA/snoRNA) transport. Surprisingly, these proteins all bind capped RNAs without strong preferences for given transcripts, and their steady-state binding correlates poorly with their function. Despite this, PHAX and ZC3H18 compete for CBC binding and we demonstrate that this competitive binding is functionally relevant. We further show that CBC-containing complexes are short lived in vivo, and we therefore suggest that RNA fate involves the transient formation of mutually exclusive CBC complexes, which may only be consequential at particular checkpoints during RNA biogenesis. RNA fate decisions RNA decay RNA transport cap RNA cap CLIP CBC CBC interacting proteins FRAP Biology (General) Nour El Houda Benbahouche verfasserin aut Michal Domanski verfasserin aut Marie-Cécile Robert verfasserin aut Nicola Meola verfasserin aut Michal Lubas verfasserin aut Jakob Bukenborg verfasserin aut Jens S. Andersen verfasserin aut Wiebke M. Schulze verfasserin aut Celine Verheggen verfasserin aut Grzegorz Kudla verfasserin aut Torben Heick Jensen verfasserin aut Edouard Bertrand verfasserin aut In Cell Reports Elsevier, 2015 18(2017), 11, Seite 2635-2650 (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:18 year:2017 number:11 pages:2635-2650 https://doi.org/10.1016/j.celrep.2017.02.046 kostenfrei https://doaj.org/article/173fd29c006e48f3b1da6b440058ecb1 kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124717302449 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 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_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 18 2017 11 2635-2650
allfieldsSound	10.1016/j.celrep.2017.02.046 doi (DE-627)DOAJ021058598 (DE-599)DOAJ173fd29c006e48f3b1da6b440058ecb1 DE-627 ger DE-627 rakwb eng QH301-705.5 Simone Giacometti verfasserin aut Mutually Exclusive CBC-Containing Complexes Contribute to RNA Fate 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The nuclear cap-binding complex (CBC) stimulates processing reactions of capped RNAs, including their splicing, 3′-end formation, degradation, and transport. CBC effects are particular for individual RNA families, but how such selectivity is achieved remains elusive. Here, we analyze three main CBC partners known to impact different RNA species. ARS2 stimulates 3′-end formation/transcription termination of several transcript types, ZC3H18 stimulates degradation of a diverse set of RNAs, and PHAX functions in pre-small nuclear RNA/small nucleolar RNA (pre-snRNA/snoRNA) transport. Surprisingly, these proteins all bind capped RNAs without strong preferences for given transcripts, and their steady-state binding correlates poorly with their function. Despite this, PHAX and ZC3H18 compete for CBC binding and we demonstrate that this competitive binding is functionally relevant. We further show that CBC-containing complexes are short lived in vivo, and we therefore suggest that RNA fate involves the transient formation of mutually exclusive CBC complexes, which may only be consequential at particular checkpoints during RNA biogenesis. RNA fate decisions RNA decay RNA transport cap RNA cap CLIP CBC CBC interacting proteins FRAP Biology (General) Nour El Houda Benbahouche verfasserin aut Michal Domanski verfasserin aut Marie-Cécile Robert verfasserin aut Nicola Meola verfasserin aut Michal Lubas verfasserin aut Jakob Bukenborg verfasserin aut Jens S. Andersen verfasserin aut Wiebke M. Schulze verfasserin aut Celine Verheggen verfasserin aut Grzegorz Kudla verfasserin aut Torben Heick Jensen verfasserin aut Edouard Bertrand verfasserin aut In Cell Reports Elsevier, 2015 18(2017), 11, Seite 2635-2650 (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:18 year:2017 number:11 pages:2635-2650 https://doi.org/10.1016/j.celrep.2017.02.046 kostenfrei https://doaj.org/article/173fd29c006e48f3b1da6b440058ecb1 kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124717302449 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 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_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 18 2017 11 2635-2650
language	English
source	In Cell Reports 18(2017), 11, Seite 2635-2650 volume:18 year:2017 number:11 pages:2635-2650
sourceStr	In Cell Reports 18(2017), 11, Seite 2635-2650 volume:18 year:2017 number:11 pages:2635-2650
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	RNA fate decisions RNA decay RNA transport cap RNA cap CLIP CBC CBC interacting proteins FRAP Biology (General)
isfreeaccess_bool	true
container_title	Cell Reports
authorswithroles_txt_mv	Simone Giacometti @@aut@@ Nour El Houda Benbahouche @@aut@@ Michal Domanski @@aut@@ Marie-Cécile Robert @@aut@@ Nicola Meola @@aut@@ Michal Lubas @@aut@@ Jakob Bukenborg @@aut@@ Jens S. Andersen @@aut@@ Wiebke M. Schulze @@aut@@ Celine Verheggen @@aut@@ Grzegorz Kudla @@aut@@ Torben Heick Jensen @@aut@@ Edouard Bertrand @@aut@@
publishDateDaySort_date	2017-01-01T00:00:00Z
hierarchy_top_id	684964562
id	DOAJ021058598
language_de	englisch
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callnumber-first	Q - Science
author	Simone Giacometti
spellingShingle	Simone Giacometti misc QH301-705.5 misc RNA fate decisions misc RNA decay misc RNA transport misc cap misc RNA cap misc CLIP misc CBC misc CBC interacting proteins misc FRAP misc Biology (General) Mutually Exclusive CBC-Containing Complexes Contribute to RNA Fate
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topic_title	QH301-705.5 Mutually Exclusive CBC-Containing Complexes Contribute to RNA Fate RNA fate decisions RNA decay RNA transport cap RNA cap CLIP CBC CBC interacting proteins FRAP
topic	misc QH301-705.5 misc RNA fate decisions misc RNA decay misc RNA transport misc cap misc RNA cap misc CLIP misc CBC misc CBC interacting proteins misc FRAP misc Biology (General)
topic_unstemmed	misc QH301-705.5 misc RNA fate decisions misc RNA decay misc RNA transport misc cap misc RNA cap misc CLIP misc CBC misc CBC interacting proteins misc FRAP misc Biology (General)
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title	Mutually Exclusive CBC-Containing Complexes Contribute to RNA Fate
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title_full	Mutually Exclusive CBC-Containing Complexes Contribute to RNA Fate
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author_browse	Simone Giacometti Nour El Houda Benbahouche Michal Domanski Marie-Cécile Robert Nicola Meola Michal Lubas Jakob Bukenborg Jens S. Andersen Wiebke M. Schulze Celine Verheggen Grzegorz Kudla Torben Heick Jensen Edouard Bertrand
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title_sort	mutually exclusive cbc-containing complexes contribute to rna fate
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title_auth	Mutually Exclusive CBC-Containing Complexes Contribute to RNA Fate
abstract	The nuclear cap-binding complex (CBC) stimulates processing reactions of capped RNAs, including their splicing, 3′-end formation, degradation, and transport. CBC effects are particular for individual RNA families, but how such selectivity is achieved remains elusive. Here, we analyze three main CBC partners known to impact different RNA species. ARS2 stimulates 3′-end formation/transcription termination of several transcript types, ZC3H18 stimulates degradation of a diverse set of RNAs, and PHAX functions in pre-small nuclear RNA/small nucleolar RNA (pre-snRNA/snoRNA) transport. Surprisingly, these proteins all bind capped RNAs without strong preferences for given transcripts, and their steady-state binding correlates poorly with their function. Despite this, PHAX and ZC3H18 compete for CBC binding and we demonstrate that this competitive binding is functionally relevant. We further show that CBC-containing complexes are short lived in vivo, and we therefore suggest that RNA fate involves the transient formation of mutually exclusive CBC complexes, which may only be consequential at particular checkpoints during RNA biogenesis.
abstractGer	The nuclear cap-binding complex (CBC) stimulates processing reactions of capped RNAs, including their splicing, 3′-end formation, degradation, and transport. CBC effects are particular for individual RNA families, but how such selectivity is achieved remains elusive. Here, we analyze three main CBC partners known to impact different RNA species. ARS2 stimulates 3′-end formation/transcription termination of several transcript types, ZC3H18 stimulates degradation of a diverse set of RNAs, and PHAX functions in pre-small nuclear RNA/small nucleolar RNA (pre-snRNA/snoRNA) transport. Surprisingly, these proteins all bind capped RNAs without strong preferences for given transcripts, and their steady-state binding correlates poorly with their function. Despite this, PHAX and ZC3H18 compete for CBC binding and we demonstrate that this competitive binding is functionally relevant. We further show that CBC-containing complexes are short lived in vivo, and we therefore suggest that RNA fate involves the transient formation of mutually exclusive CBC complexes, which may only be consequential at particular checkpoints during RNA biogenesis.
abstract_unstemmed	The nuclear cap-binding complex (CBC) stimulates processing reactions of capped RNAs, including their splicing, 3′-end formation, degradation, and transport. CBC effects are particular for individual RNA families, but how such selectivity is achieved remains elusive. Here, we analyze three main CBC partners known to impact different RNA species. ARS2 stimulates 3′-end formation/transcription termination of several transcript types, ZC3H18 stimulates degradation of a diverse set of RNAs, and PHAX functions in pre-small nuclear RNA/small nucleolar RNA (pre-snRNA/snoRNA) transport. Surprisingly, these proteins all bind capped RNAs without strong preferences for given transcripts, and their steady-state binding correlates poorly with their function. Despite this, PHAX and ZC3H18 compete for CBC binding and we demonstrate that this competitive binding is functionally relevant. We further show that CBC-containing complexes are short lived in vivo, and we therefore suggest that RNA fate involves the transient formation of mutually exclusive CBC complexes, which may only be consequential at particular checkpoints during RNA biogenesis.
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title_short	Mutually Exclusive CBC-Containing Complexes Contribute to RNA Fate
url	https://doi.org/10.1016/j.celrep.2017.02.046 https://doaj.org/article/173fd29c006e48f3b1da6b440058ecb1 http://www.sciencedirect.com/science/article/pii/S2211124717302449 https://doaj.org/toc/2211-1247
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author2Str	Nour El Houda Benbahouche Michal Domanski Marie-Cécile Robert Nicola Meola Michal Lubas Jakob Bukenborg Jens S. Andersen Wiebke M. Schulze Celine Verheggen Grzegorz Kudla Torben Heick Jensen Edouard Bertrand
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