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- Title
Ubiquitin-dependent regulation of COPII coat size and function.
- Authors
Jin, Lingyan; Pahuja, Kanika Bajaj; Wickliffe, Katherine E; Gorur, Amita; Baumgärtel, Christine; Schekman, Randy; Rape, Michael
- Abstract
Packaging of proteins from the endoplasmic reticulum into COPII vesicles is essential for secretion. In cells, most COPII vesicles are approximately 60-80 nm in diameter, yet some must increase their size to accommodate 300-400 nm procollagen fibres 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 identified the ubiquitin ligase CUL3-KLHL12 as a regulator of COPII coat formation. CUL3-KLHL12 catalyses the monoubiquitylation of the COPII-component SEC31 and drives the assembly of large COPII coats. As a result, ubiquitylation by CUL3-KLHL12 is essential for collagen export, yet less important for the transport of small cargo. We conclude that monoubiquitylation controls the size and function of a vesicle coat.
- Publication
Nature, 2012, Vol 482, Issue 7386, p495
- ISSN
1476-4687
- Publication type
Journal Article
- DOI
10.1038/nature10822