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Article

A possible effector role for the pleckstrin homology (PH) domain of dynamin.

Proceedings of the National Academy of Sciences of the United States of America - 11 Aug 2009

Bethoney Kelley A, King Megan C, Hinshaw Jenny E, Ostap E Michael, Lemmon Mark A

Abstract excerpt

The large GTPase dynamin plays a key role in clathrin-mediated endocytosis in animal cells, although its mechanism of action remains unclear. Dynamins 1, 2, and 3 contain a pleckstrin homology (PH) domain that binds phosphoinositides with a very low affinity (K(D) > 1 mM), and this interaction appears to be crucial for function. These observations prompted the suggestion that an array of PH domains drives...

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Identifiers

PMID: 19666604
DOI: 10.1073/pnas.0906945106
PMCID: PMC2720410

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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