Protein tyrosine phosphorylation and the adhesive functions of platelets.
The intracellular signalling pathways that mediate changes in cell behavior induced by extracellular matrix and cell adhesion molecules are poorly understood. Studies on the regulation of tyrosine phosphorylation in platelets indicate that cell-to-cell aggregation mediated by fibrinogen binding to its integrin-family receptor, GP IIb-IIIa, and events regulated by the putative adhesion receptor, GP IV (CD36), involve tyrosine phosphorylation. Thus, tyrosine phosphorylation is implicated in cellular events crucial for hemostasis. It may also be involved in signaling mediated by integrin receptors in other cell types.
University of Pennsylvania School of Medicine, Philadelphia.
S J
SJ
Shattil
J S
JS
Brugge
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D016023:Integrins / Q000378:metabolism; D008969:Molecular Sequence Data; D010766:Phosphorylation; D010973:Platelet Adhesiveness; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D014443:Tyrosine / Q000378:metabolism*
D016023:Integrins; D014443:Tyrosine; D011505:Protein-Tyrosine Kinases