Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis

Myosin 1E is one of two long-tailed human Class I myosins that contain an SH3 domain within the tail region. SH3 domains of yeast and amoeboid myosins I interact with activators of the Arp2/3 complex, an important regulator of actin polymerization. No binding partners for the SH3 domains of myosins I have been identified in higher eukaryotes. In the current study, we show that two proteins with prominent functions in endocytosis, synaptojanin-1 and dynamin, bind to the SH3 domain of human MyolE. Myosin IT co-localizes with clathrin- and dynamin-containing puncta at the plasma membrane and this colocalization requires an intact SH3 domain. Expression of Myo 1 E tail, which acts in a dominant-negative manner, inhibits endocytosis of transferrin. Our findings suggest that myosin 1E may contribute to receptor-mediated endocytosis. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.