| Literature DB >> 27298089 |
Charles Barlowe1, Ari Helenius2.
Abstract
Transport of newly synthesized proteins from the endoplasmic reticulum (ER) to the Golgi complex is highly selective. As a general rule, such transport is limited to soluble and membrane-associated secretory proteins that have reached properly folded and assembled conformations. To secure the efficiency, fidelity, and control of this crucial transport step, cells use a combination of mechanisms. The mechanisms are based on selective retention of proteins in the ER to prevent uptake into transport vesicles, on selective capture of proteins in COPII carrier vesicles, on inclusion of proteins in these vesicles by default as part of fluid and membrane bulk flow, and on selective retrieval of proteins from post-ER compartments by retrograde vesicle transport.Keywords: ER; Golgi; coat proteins; protein secretion; trafficking
Mesh:
Year: 2016 PMID: 27298089 DOI: 10.1146/annurev-cellbio-111315-125016
Source DB: PubMed Journal: Annu Rev Cell Dev Biol ISSN: 1081-0706 Impact factor: 13.827