Nature. 1999 Apr 8;398(6727):481-6.

Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis.

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Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, USA.

Abstract

Dynamin is a GTP-hydrolysing protein that is an essential participant in clathrin-mediated endocytosis by cells. It self-assembles into 'collars' in vitro which also formin vivo at the necks of invaginated coated pits. This self-assembly stimulates dynamin's GTPase activity and it has been proposed that dynamin hydrolyses GTP in order to generate the force needed to sever vesicles from the plasma membrane. A mechanism is now described in which self-assembly of dynamin is coordinated by a domain of dynamin with a GTPase-activating function. Unexpectedly, when dynamin mutants defective in self-assembly-stimulated GTPase activity are overexpressed, receptor-mediated endocytosis is accelerated. The results indicate that dynamin, like other members of the GTPase superfamily, functions as a molecular regulator in receptor-mediated endocytosis, rather than as a force-generating GTPase.

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Nature. 1999 Apr 8;398(6727):470-1.

PMID:: 10206643; [PubMed - indexed for MEDLINE]

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Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis.

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