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Molecular and Cellular Biology, February 1999, p. 1410-1415, Vol. 19, No. 2
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Essential Role of the Dynamin Pleckstrin Homology Domain in Receptor-Mediated Endocytosis

Mircea Achiriloaie, Barbara Barylko, and Joseph P. Albanesi*

Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas

Received 29 July 1998/Returned for modification 14 September 1998/Accepted 21 October 1998

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 beta gamma 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.

* Corresponding author. Mailing address: U.T. Southwestern Medical Center, Department of Pharmacology, 5323 Harry Hines Blvd., Dallas, TX 75235-9041. Phone: (214) 648-3200. Fax: (214) 648-2971. E-mail: joseph.albanesi{at}emailswmed.edu.

Molecular and Cellular Biology, February 1999, p. 1410-1415, Vol. 19, No. 2
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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