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PMID:22358839
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| Citation |
Jin, L, Pahuja, KB, Wickliffe, KE, Gorur, A, Baumgärtel, C, Schekman, R and Rape, M (2012) Ubiquitin-dependent regulation of COPII coat size and function. Nature 482:495-500 |
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| 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. |
| Links |
PubMed PMC3292188 Online version:10.1038/nature10822 |
| Keywords |
Animals; COP-Coated Vesicles/chemistry; COP-Coated Vesicles/metabolism; Cell Line; Cell Shape; Collagen/metabolism; Cullin Proteins/genetics; Cullin Proteins/metabolism; Embryonic Stem Cells/cytology; Embryonic Stem Cells/metabolism; HeLa Cells; Humans; Mice; Microfilament Proteins/genetics; Microfilament Proteins/metabolism; Protein Transport; Ubiquitin/metabolism; Ubiquitination; Vesicular Transport Proteins/genetics; Vesicular Transport Proteins/metabolism |
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