Tensin: a potential link between the cytoskeleton and signal transduction.
Cytoskeletal proteins provide the structural foundation that allows cells to exist in a highly organized manner. Recent evidence suggests that certain cytoskeletal proteins not only maintain structural integrity, but might also be associated with signal transduction and suppression of tumorigenesis. Since the time of the discovery of tensin, a fair amount of data has been gathered which supports the notion that tensin is one such protein possessing these characteristics. In this review, we discuss recent studies that: (1) elucidate a role for tensin in maintenance of cellular structure and signal transduction; (2) implicate tensin as the anchor for actin filaments at the focal adhesion; (3) describe the phosphorylation of tensin; (4) describe potential targets for its Src homology region 2 domain; (5) describe the association between tensin and the nuclear protein p130; and (6) demonstrate that increased tensin expression in a cell line appears to reduce its transformation potential.
Dana Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.
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D008841:Actin Cytoskeleton / Q000378:metabolism / Q000648:ultrastructure; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002448:Cell Adhesion; D002471:Cell Transformation, Neoplastic / Q000378:metabolism; D002642:Chick Embryo; D003599:Cytoskeleton / Q000502:physiology* / Q000648:ultrastructure; D051379:Mice; D008819:Mice, Nude; D008840:Microfilament Proteins / Q000737:chemistry / Q000502:physiology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D051381:Rats; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction / Q000502:physiology*; D000070876:Tensins
D008840:Microfilament Proteins; D011993:Recombinant Fusion Proteins; D000070876:Tensins; C000603372:Tns1 protein, rat