Article
Dynamin GTPase domain mutants that differentially affect GTP binding, GTP hydrolysis, and clathrin-mediated endocytosis.
The Journal of biological chemistry - 24 Sept 2004
Song Byeong Doo, Leonard Marilyn, Schmid Sandra L
Abstract excerpt
The GTPase dynamin is essential for clathrin-mediated endocytosis. Unlike most GTPases, dynamin has a low affinity for nucleotide, a high rate of GTP hydrolysis, and can self-assemble, forming higher order structures such as rings and spirals that exhibit up to 100-fold stimulated GTPase activity. The role(s) of GTP binding and/or hydrolysis in endocytosis remain unclear because mutations in the GTPase domain so...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.