Essential role of the dynamin pleckstrin homology domain in receptor- mediated endocytosis

Mircea Achiriloaie, Barbara Barylko, Joseph P. Albanesi

Research output: Contribution to journalArticlepeer-review

144 Scopus citations


Pleckstrin homology (PH) domains are found in numerous membrane- associated proteins and have been implicated in the mediation of protein- protein and protein-phospholipid interactions. Dynamin, a GTPase required for clathrin-dependent endocytosis, contains a PH domain which binds to phosphoinositides and participates in the interaction between dynamin and the βχ subunits of heterotrimeric G proteins. The PH domain is essential for expression of phosphoinositide-stimulated GTPase activity of dynamin in vitro, but its involvement in the endocytic process is unknown. We expressed a series of dynamin PH domain mutants in cultured cells and determined their effect on transferrin uptake by those cells. Endocytosis is blocked in cells expressing a PH domain deletion mutant and a point mutant that fails to interact with phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2]. In contrast, expression of a point mutant with unimpaired PI(4,5)P2 interaction has no effect on transferrin uptake. These results demonstrate the significance of the PH domain for dynamin function and suggest that its role may be to mediate interactions between dynamin and phosphoinositides.

Original languageEnglish (US)
Pages (from-to)1410-1415
Number of pages6
JournalMolecular and cellular biology
Issue number2
StatePublished - Feb 1999

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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