4.4 Article

Rab GTPase localization and Rab cascades in Golgi transport

期刊

BIOCHEMICAL SOCIETY TRANSACTIONS
卷 40, 期 -, 页码 1373-1377

出版社

PORTLAND PRESS LTD
DOI: 10.1042/BST20120168

关键词

guanine-nucleotide-dissociation inhibitor displacement factor (GDF); guanine-nucleotide-dissociation inhibitor (GDI); Golgi complex; GTPase-activating protein (GAP); guanine-nucleotide-exchange factor (GEF); Rab GTPase

资金

  1. National Institutes of Health [DK37332]

向作者/读者索取更多资源

Rab GTPases are master regulators of membrane traffic. By binding to distinct sets of effector proteins, Rabs catalyse the formation of function-specifying membrane microdomains. They are delivered to membranes by a protein named GDI (guanine-nucleotide-dissociation inhibitor) and are stabilized there after nucleotide exchange by effector binding. In the present mini-review, I discuss what we know about how Rab GTPases are delivered to the correct membrane-bound compartments and how Rab GTPase cascades order Rabs within the secretory and endocytic pathways. Finally, I describe how Rab cascades may establish the distinct compartments of the Golgi complex to permit ordered processing, sorting and secretion of secretory cargoes.

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