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Analysis of COPII Vesicles Indicates a Role for the Emp47–Ssp120 Complex in Transport of Cell Surface Glycoproteins
Author(s) -
Margulis Neil G.,
Wilson Joshua D.,
Bentivoglio Christine M.,
Dhungel Nripesh,
Gitler Aaron D.,
Barlowe Charles
Publication year - 2016
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12356
Subject(s) - copii , copi , golgi apparatus , endoplasmic reticulum , vesicle , microbiology and biotechnology , secretory pathway , biology , secretory protein , secretion , vesicular transport proteins , glycoprotein , secretory vesicle , vesicular transport protein , transport protein , biochemistry , membrane , vacuole , cytoplasm , vacuolar protein sorting
A comprehensive proteomic analysis of COPII vesicles identified the putative calcium‐binding Ssp120 protein as an efficiently packaged component of these endoplasmic reticulum ( ER )‐derived transport vesicles. Purification of Ssp120 revealed a tight association with Emp47, a transmembrane protein that contains a luminal carbohydrate recognition domain. Cell biological and genetic analyses indicated functional relationships between Ssp120 and Emp47 in trafficking. The collective findings support a model in which the Emp47–Ssp120 complex together functions as an anterograde cargo receptor for specific glycosylated secretory cargo.