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J. Biol. Chem., Vol. 281, Issue 5, 2803-2811, February 3, 2006

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Mouse Profilin 2 Regulates Endocytosis and Competes with SH3 Ligand Binding to Dynamin 1^*

Ralph Gareus, Alessia Di Nardo, Vladimir Rybin, and Walter Witke¹

From the Mouse Biology Unit, European Molecular Biology Laboratory (EMBL), Campus Adriano Buzzati-Traverso, 00016 Monterotondo, Italy and the EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany

Mammalian profilins are abundantly expressed actin monomer-binding proteins, highly conserved with respect to their affinities for G-actin, poly-L-proline, and phosphoinositides. Profilins associate with a large number of proline-rich proteins; the physiological significance and regulation of which is poorly understood. Here we show that profilin 2 associates with dynamin 1 via the C-terminal proline-rich domain of dynamin and thereby competes with the binding of SH3 ligands such as endophilin, amphiphysin, and Grb2, thus interfering with the assembly of the endocytic machinery. We also present a novel role for the brain-specific mouse profilin 2 as a regulator of membrane trafficking. Overexpression of profilin 2 inhibits endocytosis, whereas lack of profilin 2 in neurons results in an increase in endocytosis and membrane recycling. Phosphatidylinositol 4,5-bisphosphate releases profilin 2 from the profilin 2-dynamin 1 complex as well as from the profilin 2-actin complex, suggesting that profilin 2 is diverging the phosphoinositide signaling pathway to actin polymerization as well as endocytosis.

Received for publication, March 31, 2005 , and in revised form, November 28, 2005.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Tel.: 39-06-90091-268; Fax: 39-06-90091-272; E-mail: witke{at}embl-monterotondo.it.

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