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Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells

Watson, Peter Duncan, Townley, Anna K., Koka, Pratyusha, Palmer, Krysten J. and Stephens, David J. 2006. Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells. Traffic 7 (12) , pp. 1678-1687. 10.1111/j.1600-0854.2006.00493.x

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Abstract

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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Subjects: Q Science > QH Natural history > QH301 Biology
Uncontrolled Keywords: COP-coated vesicles ; COPII-coated vesicle ; endoplasmic reticulum ; Golgi apparatus ; protein transport
ISSN: 1398-9219
Last Modified: 04 Jun 2017 01:38
URI: http://orca.cf.ac.uk/id/eprint/1123

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