Journal
TRAFFIC
Volume 7, Issue 12, Pages 1678-1687Publisher
BLACKWELL PUBLISHING
DOI: 10.1111/j.1600-0854.2006.00493.x
Keywords
COP-coated vesicles; COPII-coated vesicle; endoplasmic reticulum; Golgi apparatus; protein transport
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Funding
- Medical Research Council [G117/554(71630), G117/554] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
- MRC [G117/554] Funding Source: UKRI
- Medical Research Council [G117/554] Funding Source: researchfish
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The selective export of proteins and lipids from the endoplasmic reticulum (ER) is mediated by the coat protein complex II (COPII) that assembles onto the ER membrane. In higher eukaryotes, COPII proteins assemble at discrete sites on the membrane known as ER exit sites (ERES). Here, we identify Sec16 as the protein that defines ERES in mammalian cells. Sec16 localizes to ERES independent of Sec23/24 and Sec13/31. Overexpression, and to a lesser extent, small interfering RNA depletion of Sec16, both inhibit ER-to-Golgi transport suggesting that Sec16 is required in stoichiometric amounts. Sar1 activity is required to maintain the localization of Sec16 at discrete locations on the ER membrane, probably through preventing its dissociation. Our data suggest that Sar1-GTP-dependent assembly of Sec16 on the ER membrane forms an organized scaffold defining an ERES.
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