Ubiquitin-dependent regulation of COPII coat size and function

Lingyan Jin, Kanika Bajaj Pahuja, Katherine E. Wickliffe, Amita Gorur, Christine Baumgärtel, Randy Schekman and Michael Rape ()
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Lingyan Jin: University of California at Berkeley
Kanika Bajaj Pahuja: University of California at Berkeley
Katherine E. Wickliffe: University of California at Berkeley
Amita Gorur: University of California at Berkeley
Christine Baumgärtel: University of California at Berkeley
Randy Schekman: University of California at Berkeley
Michael Rape: University of California at Berkeley

Nature, 2012, vol. 482, issue 7386, 495-500

Abstract: 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.

Date: 2012
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DOI: 10.1038/nature10822

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