| First Author | Jin L | Year | 2012 |
| Journal | Nature | Volume | 482 |
| Issue | 7386 | Pages | 495-500 |
| PubMed ID | 22358839 | Mgi Jnum | J:181630 |
| Mgi Id | MGI:5312166 | Doi | 10.1038/nature10822 |
| Citation | Jin L, et al. (2012) Ubiquitin-dependent regulation of COPII coat size and function. Nature 482(7386):495-500 |
| abstractText | 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. |
