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New Insights into the Structural Mechanisms of the COPII Coat
Author(s) -
Russell Christopher,
Stagg Scott M.
Publication year - 2010
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/j.1600-0854.2009.01026.x
Subject(s) - copii , copi , endoplasmic reticulum , biology , vesicular transport proteins , microbiology and biotechnology , golgi apparatus , coat protein , transport protein , secretory pathway , biochemistry , rna , gene , vacuolar protein sorting , endosome , intracellular
In eukaryotes, coat protein complex II (COPII) proteins are involved in transporting cargo proteins from the endoplasmic reticulum (ER) to the Golgi apparatus. The COPII proteins, Sar1, Sec23/24, and Sec13/31 polymerize into a coat that gathers cargo proteins into a coated vesicle. Structures have been recently solved of individual COPII proteins, COPII proteins in complex with cargo, and higher‐order COPII coat assemblies. In this review, we will summarize the latest developments in COPII structure and discuss how these structures shed light on the functional mechanisms of the COPII coat.