Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 40, Issue -, Pages 1373-1377Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST20120168
Keywords
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
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Funding
- National Institutes of Health [DK37332]
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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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