Tyrosine phosphorylation of the focal adhesion kinase pp125FAK during development: relation to paxillin.

Abstract

Significant changes in the level of protein tyrosine phosphorylation accompany avian embryonic development. A comparison of different tissues reveals that a similar and remarkably restricted complement of proteins is modified in this manner. In each case the major proteins detected using anti-phosphotyrosine antibodies have molecular masses of approximately 170, 150, 125, 70 and 50 kDa. As a first step in determining the function of this protein modification in embryogenesis we have initiated a study to identify these phosphoproteins. We have previously reported that the 70 kDa band is paxillin, a component of actin-membrane attachment sites associated with regions of cell adhesion (Turner, C. E. (1991) J. Cell Biol. 115, 201-207). We report here that the 125 kDa phosphotyrosine-containing protein is the tyrosine kinase pp125FAK, a protein that co-localizes with paxillin at sites of adhesion (Schaller et al. (1992) Proc. Nat. Acad. Sci. USA 89, 5192-5196). Tyrosine phosphorylation of both pp125FAK and paxillin was detected at low levels as early as embryonic day 3 and increased steadily during the first half of development, reached a maximum between embryonic days eight and twelve, and declined to background levels prior to hatching. Paxillin protein expression also increased during the first half of embryogenesis, suggesting little change in the overall phosphorylation of this protein through embryonic day 8. In contrast, pp125FAK, following an initial increase, is expressed at a constant high level during these early embryonic stages, implying an increase in its overall phosphotyrosine content.(ABSTRACT TRUNCATED AT 250 WORDS)