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

Mira Krendel1, Emily K Osterweil, Mark S Mooseker

  • 1Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06511, USA. mira.krendel@yale.edu

FEBS Letters
|January 30, 2007
PubMed

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 Myo1E. Myosin 1E co-localizes with clathrin- and dynamin-containing puncta at the plasma membrane and this co-localization requires an intact SH3 domain. Expression of Myo1E tail, which acts in a dominant-negative manner, inhibits endocytosis of transferrin. Our findings suggest that myosin 1E may contribute to receptor-mediated endocytosis.

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