Paxillin: a cytoskeletal target for tyrosine kinases.
Paxillin is a recently identified member of the complex of cytoskeletal proteins that is found concentrated in cultured cells and in vivo at the cytoplasmic face of regions of cell attachment to the extracellular matrix. These sites, in view of their close proximity to the extracellular matrix, are well positioned to act as signal-transducing centers to 'report on' changes in the cells, immediate environment. Recent findings indicate that such signals are in part mediated through the activation of tyrosine kinases concentrated at the sites of adhesion. Changes in the phosphotyrosine content of paxillin accompanying this elevation in kinase activity suggest that paxillin may be an important intermediary in these pathways.
Turner
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Department of Anatomy and Cell Biology, SUNY Health Science Center, Syracuse 13210.
D000818:Animals; D002448:Cell Adhesion; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D003599:Cytoskeleton / Q000502:physiology*; D005314:Embryonic and Fetal Development / Q000502:physiology; D005109:Extracellular Matrix / Q000502:physiology; D051419:Paxillin; D010750:Phosphoproteins / Q000378:metabolism*; D019000:Phosphotyrosine; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D015398:Signal Transduction; D014443:Tyrosine / Q000031:analogs & derivatives / Q000378:metabolism; D016596:Vinculin / Q000378:metabolism
D003598:Cytoskeletal Proteins; D051419:Paxillin; D010750:Phosphoproteins; D016596:Vinculin; D019000:Phosphotyrosine; D014443:Tyrosine; D011505:Protein-Tyrosine Kinases