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

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.

• Authors: Yuqing Liu, Lizhao Guan, Jun Zhan, Danyu Lu, Junhu Wan, Hongquan Zhang
• Journal: FEBS letters (FEBS Lett) Vol. 588 Issue 17 Pg. 2859-66 (Aug 25 2014) ISSN: 1873-3468 [Electronic] England
• PMID: 24997346 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Chemical References

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

Topics

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