Phosphotyrosine signalling as a regulator of neural crest cell adhesion and motility.

摘要: We demonstrate that neural crest cell-cell adhesion, cell-substrate and ultimately cell motility, are highly dependent on the balanced action of tyrosine kinases phosphatases. Neural migration fibronectin is diminished in presence phosphatase inhibitor vanadate or kinase herbimycin A, while cadherin-rich adhesions significantly increased. In contrast, cells treated with genistein have decreased rearrange rapidly reversibly into a pavement-like monolayer, but no increase cadherin interactions. Genistein-sensitive may therefore abrogate latent sensitivity to contact-mediated inhibition movement. Furthermore, we show activity A-sensitive necessary for focal adhesion formation these cells. Moreover, size distribution acutely sensitive actions phosphatases genistein-sensitive kinases. propose migrating there balance phosphotyrosine signalling which minimises both contact movement, enhancing dynamic interactions thus conditions motility. Cell Motil. Cytoskeleton 42:101–113, 1999. © 1999 Wiley-Liss, Inc.