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Broadly conserved roles of TMEM131 family proteins in intracellular collagen assembly and secretory cargo trafficking
Collagen is the most abundant protein in animals. Its dysregulation contributes to aging and many human disorders, including pathological tissue fibrosis in major organs. How premature collagen proteins in the endoplasmic reticulum (ER) assemble and route for secretion remains molecularly undefined....
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Association for the Advancement of Science
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7015688/ https://www.ncbi.nlm.nih.gov/pubmed/32095531 http://dx.doi.org/10.1126/sciadv.aay7667 |
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author | Zhang, Zhe Bai, Meirong Barbosa, Guilherme Oliveira Chen, Andrew Wei, Yuehua Luo, Shuo Wang, Xin Wang, Bingying Tsukui, Tatsuya Li, Hao Sheppard, Dean Kornberg, Thomas B. Ma, Dengke K. |
author_facet | Zhang, Zhe Bai, Meirong Barbosa, Guilherme Oliveira Chen, Andrew Wei, Yuehua Luo, Shuo Wang, Xin Wang, Bingying Tsukui, Tatsuya Li, Hao Sheppard, Dean Kornberg, Thomas B. Ma, Dengke K. |
author_sort | Zhang, Zhe |
collection | PubMed |
description | Collagen is the most abundant protein in animals. Its dysregulation contributes to aging and many human disorders, including pathological tissue fibrosis in major organs. How premature collagen proteins in the endoplasmic reticulum (ER) assemble and route for secretion remains molecularly undefined. From an RNA interference screen, we identified an uncharacterized Caenorhabditis elegans gene tmem-131, deficiency of which impairs collagen production and activates ER stress response. We find that amino termini of human TMEM131 contain bacterial PapD chaperone–like domains, which recruit premature collagen monomers for proper assembly and secretion. Carboxy termini of TMEM131 interact with TRAPPC8, a component of the TRAPP tethering complex, to drive collagen cargo trafficking from ER to the Golgi. We provide evidence that previously undescribed roles of TMEM131 in collagen recruitment and secretion are evolutionarily conserved in C. elegans, Drosophila, and humans. |
format | Online Article Text |
id | pubmed-7015688 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-70156882020-02-24 Broadly conserved roles of TMEM131 family proteins in intracellular collagen assembly and secretory cargo trafficking Zhang, Zhe Bai, Meirong Barbosa, Guilherme Oliveira Chen, Andrew Wei, Yuehua Luo, Shuo Wang, Xin Wang, Bingying Tsukui, Tatsuya Li, Hao Sheppard, Dean Kornberg, Thomas B. Ma, Dengke K. Sci Adv Research Articles Collagen is the most abundant protein in animals. Its dysregulation contributes to aging and many human disorders, including pathological tissue fibrosis in major organs. How premature collagen proteins in the endoplasmic reticulum (ER) assemble and route for secretion remains molecularly undefined. From an RNA interference screen, we identified an uncharacterized Caenorhabditis elegans gene tmem-131, deficiency of which impairs collagen production and activates ER stress response. We find that amino termini of human TMEM131 contain bacterial PapD chaperone–like domains, which recruit premature collagen monomers for proper assembly and secretion. Carboxy termini of TMEM131 interact with TRAPPC8, a component of the TRAPP tethering complex, to drive collagen cargo trafficking from ER to the Golgi. We provide evidence that previously undescribed roles of TMEM131 in collagen recruitment and secretion are evolutionarily conserved in C. elegans, Drosophila, and humans. American Association for the Advancement of Science 2020-02-12 /pmc/articles/PMC7015688/ /pubmed/32095531 http://dx.doi.org/10.1126/sciadv.aay7667 Text en Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). http://creativecommons.org/licenses/by-nc/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (http://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited. |
spellingShingle | Research Articles Zhang, Zhe Bai, Meirong Barbosa, Guilherme Oliveira Chen, Andrew Wei, Yuehua Luo, Shuo Wang, Xin Wang, Bingying Tsukui, Tatsuya Li, Hao Sheppard, Dean Kornberg, Thomas B. Ma, Dengke K. Broadly conserved roles of TMEM131 family proteins in intracellular collagen assembly and secretory cargo trafficking |
title | Broadly conserved roles of TMEM131 family proteins in intracellular collagen assembly and secretory cargo trafficking |
title_full | Broadly conserved roles of TMEM131 family proteins in intracellular collagen assembly and secretory cargo trafficking |
title_fullStr | Broadly conserved roles of TMEM131 family proteins in intracellular collagen assembly and secretory cargo trafficking |
title_full_unstemmed | Broadly conserved roles of TMEM131 family proteins in intracellular collagen assembly and secretory cargo trafficking |
title_short | Broadly conserved roles of TMEM131 family proteins in intracellular collagen assembly and secretory cargo trafficking |
title_sort | broadly conserved roles of tmem131 family proteins in intracellular collagen assembly and secretory cargo trafficking |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7015688/ https://www.ncbi.nlm.nih.gov/pubmed/32095531 http://dx.doi.org/10.1126/sciadv.aay7667 |
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