Myosin VI is required for E-cadherin-mediated border cell migration

• Published in: Nature cell biology Vol. 4; no. 8; pp. 616 - 620
• Main Authors: Montell, Denise J, Geisbrecht, Erika R
• Format: Journal Article
• Language: English
• Published: England Nature Publishing Group 01.08.2002
• Subjects: Animals; Animals, Genetically Modified; Armadillo Domain Proteins; beta Catenin; Cadherins - metabolism; Cell adhesion & migration; Cell migration; Cell Movement - physiology; Cytoskeletal Proteins - metabolism; Drosophila melanogaster - cytology; Drosophila melanogaster - genetics; Drosophila melanogaster - metabolism; Drosophila Proteins - genetics; Drosophila Proteins - metabolism; Female; Follicles; Hair; Insect Proteins - metabolism; Insects; Membrane proteins; Molecular Motor Proteins - genetics; Molecular Motor Proteins - metabolism; Mutation; Myosin; Myosin Heavy Chains - genetics; Myosin Heavy Chains - metabolism; Ovaries; Ovary - cytology; Ovary - metabolism; Physiological aspects; Proteins; Trans-Activators - metabolism; Transcription Factors
• ISSN: 1465-7392; 1476-4679; 1476-4679
• DOI: 10.1038/ncb830

Myosin VI (MyoVI) is a pointed-end-directed, actin-based motor protein, and mutations in the gene result in disorganization of hair cell stereocilia and cause deafness in mice. MyoVI also localizes to the leading edges of growth-factor-stimulated fibroblast cells and has been suggested to be involved in cell motility. There has been no direct test of this hypothesis, however. Drosophila melanogaster MyoVI is expressed in a small group of migratory follicle cells, known as border cells. Here we show that depletion of MyoVI specifically from border cells severely inhibited their migration. Similar to MyoVI, E-cadherin is required for border cell migration. We found that E-cadherin and Armadillo (Arm, Drosophila β-catenin) protein levels were specifically reduced in cells lacking MyoVI, whereas other proteins were not. In addition, MyoVI protein levels were reduced in cells lacking DE-cadherin or Arm. MyoVI and Arm co-immunoprecipitated from ovarian protein extracts. These data suggest that MyoVI is required for border cell migration where it stabilizes E-cadherin and Arm. Mutations in MyoVIIA, another unconventional myosin protein, also lead to deafness, and MyoVIIA interacts with E-cadherin through a membrane protein called vezatin. Multiple biochemical mechanisms may exist, therefore, for cadherins to associate with diverse unconventional myosins that are required for normal stereocilium formation or maintenance.