FERM domain-containing unconventional myosin VIIA interacts with integrin β5 subunit and regulates αvβ5-mediated cell adhesion and migration

FEBS Lett. 2014 Aug 25;588(17):2859-66. doi: 10.1016/j.febslet.2014.06.049. Epub 2014 Jul 2.

Abstract

Unconventional myosin VIIA (Myo7a) has been known to associate with hereditary deafness. Here we present a novel function of Myo7a by identifying that Myo7a directly interacts with integrin β5 subunit and regulates cell adhesion and motility in an integrin-dependent manner. We found that Myo7a bound to the cytoplasmic tail of integrin β5. Further, we pinpointed an integrin-binding domain at F3 of the first FERM domain and F1 of the second FERM domain. Functionally, Myo7a-induced cell adhesion and migration were mediated by integrin αvβ5. These findings indicated that Myo7a interacts with integrin β5 and selectively promotes integrin αvβ5-mediated cell migration.

Keywords: Cell adhesion; Cell migration; Hereditary deafness; Integrin β5 subunit; Myosin VIIA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Adhesion
  • Cell Line
  • Cell Movement*
  • Cytoplasm / metabolism
  • Humans
  • Integrin beta Chains / metabolism*
  • Mice
  • Myosin VIIa
  • Myosins / chemistry*
  • Myosins / metabolism*
  • Protein Binding
  • Protein Structure, Tertiary
  • Receptors, Vitronectin / metabolism*

Substances

  • Integrin beta Chains
  • MYO7A protein, human
  • Myo7a protein, mouse
  • Myosin VIIa
  • Receptors, Vitronectin
  • integrin alphaVbeta5
  • integrin beta5
  • Myosins