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A new role for RINT-1 in SNARE complex assembly at the trans-Golgi network in coordination with the COG complex
Docking and fusion of transport vesicles/carriers with the target membrane involve a tethering factor–mediated initial contact followed by soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE)–catalyzed membrane fusion. The multisubunit tethering CATCHR family complexes (Dsl1...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3771952/ https://www.ncbi.nlm.nih.gov/pubmed/23885118 http://dx.doi.org/10.1091/mbc.E13-01-0014 |
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author | Arasaki, Kohei Takagi, Daichi Furuno, Akiko Sohda, Miwa Misumi, Yoshio Wakana, Yuichi Inoue, Hiroki Tagaya, Mitsuo |
author_facet | Arasaki, Kohei Takagi, Daichi Furuno, Akiko Sohda, Miwa Misumi, Yoshio Wakana, Yuichi Inoue, Hiroki Tagaya, Mitsuo |
author_sort | Arasaki, Kohei |
collection | PubMed |
description | Docking and fusion of transport vesicles/carriers with the target membrane involve a tethering factor–mediated initial contact followed by soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE)–catalyzed membrane fusion. The multisubunit tethering CATCHR family complexes (Dsl1, COG, exocyst, and GARP complexes) share very low sequence homology among subunits despite likely evolving from a common ancestor and participate in fundamentally different membrane trafficking pathways. Yeast Tip20, as a subunit of the Dsl1 complex, has been implicated in retrograde transport from the Golgi apparatus to the endoplasmic reticulum. Our previous study showed that RINT-1, the mammalian counterpart of yeast Tip20, mediates the association of ZW10 (mammalian Dsl1) with endoplasmic reticulum–localized SNARE proteins. In the present study, we show that RINT-1 is also required for endosome-to–trans-Golgi network trafficking. RINT-1 uncomplexed with ZW10 interacts with the COG complex, another member of the CATCHR family complex, and regulates SNARE complex assembly at the trans-Golgi network. This additional role for RINT-1 may in part reflect adaptation to the demand for more diverse transport routes from endosomes to the trans-Golgi network in mammals compared with those in a unicellular organism, yeast. The present findings highlight a new role of RINT-1 in coordination with the COG complex. |
format | Online Article Text |
id | pubmed-3771952 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-37719522013-11-30 A new role for RINT-1 in SNARE complex assembly at the trans-Golgi network in coordination with the COG complex Arasaki, Kohei Takagi, Daichi Furuno, Akiko Sohda, Miwa Misumi, Yoshio Wakana, Yuichi Inoue, Hiroki Tagaya, Mitsuo Mol Biol Cell Articles Docking and fusion of transport vesicles/carriers with the target membrane involve a tethering factor–mediated initial contact followed by soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE)–catalyzed membrane fusion. The multisubunit tethering CATCHR family complexes (Dsl1, COG, exocyst, and GARP complexes) share very low sequence homology among subunits despite likely evolving from a common ancestor and participate in fundamentally different membrane trafficking pathways. Yeast Tip20, as a subunit of the Dsl1 complex, has been implicated in retrograde transport from the Golgi apparatus to the endoplasmic reticulum. Our previous study showed that RINT-1, the mammalian counterpart of yeast Tip20, mediates the association of ZW10 (mammalian Dsl1) with endoplasmic reticulum–localized SNARE proteins. In the present study, we show that RINT-1 is also required for endosome-to–trans-Golgi network trafficking. RINT-1 uncomplexed with ZW10 interacts with the COG complex, another member of the CATCHR family complex, and regulates SNARE complex assembly at the trans-Golgi network. This additional role for RINT-1 may in part reflect adaptation to the demand for more diverse transport routes from endosomes to the trans-Golgi network in mammals compared with those in a unicellular organism, yeast. The present findings highlight a new role of RINT-1 in coordination with the COG complex. The American Society for Cell Biology 2013-09-15 /pmc/articles/PMC3771952/ /pubmed/23885118 http://dx.doi.org/10.1091/mbc.E13-01-0014 Text en © 2013 Arasaki et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Arasaki, Kohei Takagi, Daichi Furuno, Akiko Sohda, Miwa Misumi, Yoshio Wakana, Yuichi Inoue, Hiroki Tagaya, Mitsuo A new role for RINT-1 in SNARE complex assembly at the trans-Golgi network in coordination with the COG complex |
title | A new role for RINT-1 in SNARE complex assembly at the trans-Golgi network in coordination with the COG complex |
title_full | A new role for RINT-1 in SNARE complex assembly at the trans-Golgi network in coordination with the COG complex |
title_fullStr | A new role for RINT-1 in SNARE complex assembly at the trans-Golgi network in coordination with the COG complex |
title_full_unstemmed | A new role for RINT-1 in SNARE complex assembly at the trans-Golgi network in coordination with the COG complex |
title_short | A new role for RINT-1 in SNARE complex assembly at the trans-Golgi network in coordination with the COG complex |
title_sort | new role for rint-1 in snare complex assembly at the trans-golgi network in coordination with the cog complex |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3771952/ https://www.ncbi.nlm.nih.gov/pubmed/23885118 http://dx.doi.org/10.1091/mbc.E13-01-0014 |
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