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Published 3 July 2006. doi:10.1083/jcb.200604058
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 174, Number 1, 53-63
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Article

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



Yusong Guo and Adam D. Linstedt

Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15213

Correspondence to Adam D. Linstedt: linstedt{at}andrew.cmu.edu

Under experimental conditions, the Golgi apparatus can undergo de novo biogenesis from the endoplasmic reticulum (ER), involving a rapid phase of growth followed by a return to steady state, but the mechanisms that control growth are unknown. Quantification 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.

Abbreviations used in this paper: BFA, brefeldin A; COP, coat protein complex; GalNAcT2, N-acetylgalactosaminyl transferase-2; NRK, normal rat kidney; VSVG, vesicular stomatitus virus G protein; VTC, vesicular-tubular cluster.


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