Ubiquitin-dependent regulation of COPII coat size and function

Packaging of proteins from the ER into COPII-vesicles is essential for secretion. In cells, most COPII-vesicles are ~60-80nm in diameter, yet some must increase their size to accommodate 300-400nm procollagen fibers or chylomicrons. Impaired COPII function results in collagen deposition defects, cra...

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Autores principales: Jin, Lingyan, Pahuja, Kanika Bajaj, Wickliffe, Katherine E., Gorur, Amita, Baumgärtel, Christine, Schekman, Randy, Rape, Michael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2012
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3292188/
https://www.ncbi.nlm.nih.gov/pubmed/22358839
http://dx.doi.org/10.1038/nature10822
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author Jin, Lingyan
Pahuja, Kanika Bajaj
Wickliffe, Katherine E.
Gorur, Amita
Baumgärtel, Christine
Schekman, Randy
Rape, Michael
author_facet Jin, Lingyan
Pahuja, Kanika Bajaj
Wickliffe, Katherine E.
Gorur, Amita
Baumgärtel, Christine
Schekman, Randy
Rape, Michael
author_sort Jin, Lingyan
collection PubMed
description Packaging of proteins from the ER into COPII-vesicles is essential for secretion. In cells, most COPII-vesicles are ~60-80nm in diameter, yet some must increase their size to accommodate 300-400nm procollagen fibers or chylomicrons. Impaired COPII function results in collagen deposition defects, cranio-lenticulo-sutural dysplasia, or chylomicron retention disease, but mechanisms to enlarge COPII-coats have remained elusive. Here, we have identified the ubiquitin ligase Cul3(Klhl12) as a regulator of COPII coat formation. Cul3(Klhl12) catalyzes the monoubiquitination of the COPII-component Sec31 and drives the assembly of large COPII coats. As a result, ubiquitination by Cul3(Klhl12) is essential for collagen export, yet less important for the transport of small cargo. We conclude that monoubiquitination controls the size and function of a vesicle coat.
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spelling pubmed-32921882012-08-23 Ubiquitin-dependent regulation of COPII coat size and function Jin, Lingyan Pahuja, Kanika Bajaj Wickliffe, Katherine E. Gorur, Amita Baumgärtel, Christine Schekman, Randy Rape, Michael Nature Article Packaging of proteins from the ER into COPII-vesicles is essential for secretion. In cells, most COPII-vesicles are ~60-80nm in diameter, yet some must increase their size to accommodate 300-400nm procollagen fibers or chylomicrons. Impaired COPII function results in collagen deposition defects, cranio-lenticulo-sutural dysplasia, or chylomicron retention disease, but mechanisms to enlarge COPII-coats have remained elusive. Here, we have identified the ubiquitin ligase Cul3(Klhl12) as a regulator of COPII coat formation. Cul3(Klhl12) catalyzes the monoubiquitination of the COPII-component Sec31 and drives the assembly of large COPII coats. As a result, ubiquitination by Cul3(Klhl12) is essential for collagen export, yet less important for the transport of small cargo. We conclude that monoubiquitination controls the size and function of a vesicle coat. 2012-02-22 /pmc/articles/PMC3292188/ /pubmed/22358839 http://dx.doi.org/10.1038/nature10822 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Jin, Lingyan
Pahuja, Kanika Bajaj
Wickliffe, Katherine E.
Gorur, Amita
Baumgärtel, Christine
Schekman, Randy
Rape, Michael
Ubiquitin-dependent regulation of COPII coat size and function
title Ubiquitin-dependent regulation of COPII coat size and function
title_full Ubiquitin-dependent regulation of COPII coat size and function
title_fullStr Ubiquitin-dependent regulation of COPII coat size and function
title_full_unstemmed Ubiquitin-dependent regulation of COPII coat size and function
title_short Ubiquitin-dependent regulation of COPII coat size and function
title_sort ubiquitin-dependent regulation of copii coat size and function
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3292188/
https://www.ncbi.nlm.nih.gov/pubmed/22358839
http://dx.doi.org/10.1038/nature10822
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