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

Sanja Sever, Amy B. Muhlberg and Sandra L. Schmid ()
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Sanja Sever: The Scripps Research Institute
Amy B. Muhlberg: The Scripps Research Institute
Sandra L. Schmid: The Scripps Research Institute

Nature, 1999, vol. 398, issue 6727, 481-486

Abstract: 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 form in 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.

Date: 1999
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DOI: 10.1038/19024

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