期刊
JOURNAL OF CELL SCIENCE
卷 129, 期 8, 页码 1537-1545出版社
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.183335
关键词
Anterograde transport; Retrograde transport; Cargo capture; Membrane proteins; Partitioning; Sorting signals
类别
资金
- Italian National Research Council
- Regione Lombardia [MbMM-convenzioneno. 18099/RCC]
- Italian Association for Cancer Research (AIRC) [2009]
- University of Milan
- Monzino Foundation
- Confalonieri Foundation
Secretory proteins exit the endoplasmic reticulum (ER) in coat protein complex II (COPII)-coated vesicles and then progress through the Golgi complex before delivery to their final destination. Soluble cargo can be recruited to ER exit sites by signal-mediated processes (cargo capture) or by bulk flow. For membrane proteins, a third mechanism, based on the interaction of their transmembrane domain (TMD) with lipid microdomains, must also be considered. In this Commentary, I review evidence in favor of the idea that partitioning of TMDs into bilayer domains that are endowed with distinct physico-chemical properties plays a pivotal role in the transport of membrane proteins within the early secretory pathway. The combination of such self-organizational phenomena with canonical intermolecular interactions is most likely to control the release of membrane proteins from the ER into the secretory pathway.
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