Tyrosine phosphorylation of pp125FAK in platelets requires coordinated signaling through integrin and agonist receptors
Sanford J. Shattil,Beatrice Haimovich,Michael E. Cunningham,Lorraine Lipfert,J T Parsons,Mark H. Ginsberg,Joan S. Brugge +6 more
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TL;DR: In this article, the authors examined the conditions that stimulate or inhibit FAK phosphorylation in platelets in which fibrinogen binding to alpha IIb beta 3 and platelet aggregation were induced directly with an anti-beta 3 Fab fragment (anti-LIBS6).
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About: This article is published in Journal of Biological Chemistry. The article was published on 20 May 1994. and is currently open access. The article focuses on the topics: Tyrosine phosphorylation & Platelet activation.
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The bisindolylmaleimide GF 109203X is a potent and selective inhibitor of protein kinase C.
D Toullec,P Pianetti,H Coste,P Bellevergue,T Grand-Perret,M Ajakane,V Baudet,P Boissin,E Boursier,F Loriolle +9 more
TL;DR: GF 109203X was a competitive inhibitor with respect to ATP and displayed high selectivity for PKC as compared to five different protein kinases, illustrating the potential of this compound as a tool for studying the involvement of PKC in signal transduction pathways.
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pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions.
TL;DR: The isolation of a cDNA encoding a protein, pp125, that is a major phosphotyrosine-containing protein in untransformed chicken embryo cells and exhibits an increase in phosphotYrosine in pp60v-src-transformedChicken embryo cells is reported.
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Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly.
TL;DR: A role for integrin- mediated tyrosine phosphorylation in the organization of the cytoskeleton as cells adhere to the extracellular matrix is suggested.