Please use this identifier to cite or link to this item: http://hdl.handle.net/1783.1/67419

COPII-Golgi protein interactions regulate COPII coat assembly and Golgi size

Authors Guo, Yusong View this author's profile
Linstedt, Adam D.
Issue Date 2006
Source Journal of Cell Biology , v. 174, Issue 1, 3 July 2006, p. 53-63
Summary Under experimental conditions, the Golgi apparatus can undergo de novo biogenesis from the en doplasmic reticulum (ER), involving a rapid phase of growth followed by a return to steady state, but the mechanisms that control growth are unknown. Quanti. cation of coat protein complex (COP) II assembly revealed a dramatic up-regulation at exit sites driven by increased levels of Golgi proteins in the ER. Analysis in a permeabilized cell assay indicated that up-regulation of COPII assembly occurred in the absence GTP hydrolysis and any cytosolic factors other than the COPII prebudding complex Sar1p-Sec23p-Sec24p. Remarkably, acting via a direct interaction with Sar1p, increased expression of the Golgi enzyme N-acetylgalactosaminyl transferase-2 induced increased COPII assembly on the ER and an overall increase in the size of the Golgi apparatus. These results suggest that direct interactions between Golgi proteins exiting the ER and COPII components regulate ER exit, providing a variable exit rate mechanism that ensures homeostasis of the Golgi apparatus. © The Rockefeller University Press.
ISSN 00219525
Language English
Format Article
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