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

FEBS Lett. 2007 Feb 20;581(4):644-50. doi: 10.1016/j.febslet.2007.01.021. Epub 2007 Jan 18.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Animals
  • COS Cells
  • Chlorocebus aethiops
  • Clathrin-Coated Vesicles / metabolism
  • Dynamins / metabolism*
  • Endocytosis*
  • HeLa Cells
  • Humans
  • Immunoprecipitation
  • Mice
  • Myosin Type I / chemistry
  • Myosin Type I / metabolism*
  • Nerve Tissue Proteins / metabolism*
  • Phosphoric Monoester Hydrolases / metabolism*
  • Protein Binding
  • Protein Transport
  • Rats
  • Synapses / metabolism
  • Tissue Extracts
  • Transferrin / metabolism
  • Two-Hybrid System Techniques
  • src Homology Domains


  • Nerve Tissue Proteins
  • Tissue Extracts
  • Transferrin
  • synaptojanin
  • Phosphoric Monoester Hydrolases
  • MYO1E protein, human
  • Myosin Type I
  • Dynamins