Journal
JOURNAL OF CELL BIOLOGY
Volume 174, Issue 1, Pages 53-63Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200604058
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Funding
- NIGMS NIH HHS [GM-56779, R01 GM056779] Funding Source: Medline
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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.
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