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Gene Review

Tln1  -  talin 1

Mus musculus

Synonyms: Talin-1, Tln
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Disease relevance of Tln1


High impact information on Tln1


Biological context of Tln1


Anatomical context of Tln1


Associations of Tln1 with chemical compounds

  • Talin binding disrupts the salt bridge between the alpha/beta tails, leading to tail separation and integrin activation [14].
  • Indeed, binding of talin present in rat brain extracts to a glutathione S-transferase integrin beta1-cytodomain polypeptide was inhibited by the PIP kinase peptide [10].
  • Recently, the integrin beta3 cytodomain and phosphatidylinositol phosphate (PIP) kinase type 1gamma (a phosphatidylinositol 4,5-bisphosphate-synthesizing enzyme) were shown to bind to the talin FERM domain (subdomain F3) [10].
  • Two tyrosine residues flanking the SPLH motif (Tyr-644 and Tyr-649) have been implicated in the regulation of talin binding [15].
  • Modeling studies suggest that phosphorylation of Tyr-649 will likewise have little effect on talin binding, whereas phosphorylation of the SPLH serine is predicted to be strongly disruptive [15].

Physical interactions of Tln1

  • Phosphatidylinositol phosphate kinase type 1gamma and beta1-integrin cytoplasmic domain bind to the same region in the talin FERM domain [10].
  • Isolation of peptides from phage-displayed random peptide libraries that interact with the talin-binding domain of vinculin [8].
  • We show that talin physically interacts with CR3/alpha(M)beta(2) and that this interaction involves the talin head domain and residues W747 and F754 in the beta(2) integrin cytoplasmic domain [16].

Enzymatic interactions of Tln1


Regulatory relationships of Tln1

  • Talin immunostaining was widespread throughout control cells but was localized to the periphery 8 h after treatment with TPA or with inhibitors of PKC and calpain [18].
  • This suggests that the local association of talin with these sites is induced by the cytoplasmic tail of beta 1 integrin receptor presented by the chimeric protein [19].
  • These combined results suggest a model in which the reciprocal actions of Src tyrosine kinase and Shp-1 tyrosine phosphatase dynamically regulate the association between PIPKI gamma661 and talin [20].

Other interactions of Tln1


Analytical, diagnostic and therapeutic context of Tln1


  1. Clostridium difficile toxin B induces reorganization of actin, vinculin, and talin in cultured cells. Ottlinger, M.E., Lin, S. Exp. Cell Res. (1988) [Pubmed]
  2. Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate. Gilmore, A.P., Burridge, K. Nature (1996) [Pubmed]
  3. The molecular basis of filamin binding to integrins and competition with talin. Kiema, T., Lad, Y., Jiang, P., Oxley, C.L., Baldassarre, M., Wegener, K.L., Campbell, I.D., Ylänne, J., Calderwood, D.A. Mol. Cell (2006) [Pubmed]
  4. Activation of protein kinase C results in the displacement of its myristoylated, alanine-rich substrate from punctate structures in macrophage filopodia. Rosen, A., Keenan, K.F., Thelen, M., Nairn, A.C., Aderem, A. J. Exp. Med. (1990) [Pubmed]
  5. Colocalization of F-actin and talin during Fc receptor-mediated phagocytosis in mouse macrophages. Greenberg, S., Burridge, K., Silverstein, S.C. J. Exp. Med. (1990) [Pubmed]
  6. Talin requires beta-integrin, but not vinculin, for its assembly into focal adhesion-like structures in the nematode Caenorhabditis elegans. Moulder, G.L., Huang, M.M., Waterston, R.H., Barstead, R.J. Mol. Biol. Cell (1996) [Pubmed]
  7. Integrin-mediated cell adhesion: the cytoskeletal connection. Critchley, D.R., Holt, M.R., Barry, S.T., Priddle, H., Hemmings, L., Norman, J. Biochem. Soc. Symp. (1999) [Pubmed]
  8. Isolation of peptides from phage-displayed random peptide libraries that interact with the talin-binding domain of vinculin. Adey, N.B., Kay, B.K. Biochem. J. (1997) [Pubmed]
  9. Calpain-mediated proteolysis of talin regulates adhesion dynamics. Franco, S.J., Rodgers, M.A., Perrin, B.J., Han, J., Bennin, D.A., Critchley, D.R., Huttenlocher, A. Nat. Cell Biol. (2004) [Pubmed]
  10. Phosphatidylinositol phosphate kinase type 1gamma and beta1-integrin cytoplasmic domain bind to the same region in the talin FERM domain. Barsukov, I.L., Prescot, A., Bate, N., Patel, B., Floyd, D.N., Bhanji, N., Bagshaw, C.R., Letinic, K., Di Paolo, G., De Camilli, P., Roberts, G.C., Critchley, D.R. J. Biol. Chem. (2003) [Pubmed]
  11. Regulation of adherens junction protein expression in growth-activated 3T3 cells and in regenerating liver. Glück, U., Rodríguez Fernández, J.L., Pankov, R., Ben-Ze'ev, A. Exp. Cell Res. (1992) [Pubmed]
  12. Disruption of the talin gene compromises focal adhesion assembly in undifferentiated but not differentiated embryonic stem cells. Priddle, H., Hemmings, L., Monkley, S., Woods, A., Patel, B., Sutton, D., Dunn, G.A., Zicha, D., Critchley, D.R. J. Cell Biol. (1998) [Pubmed]
  13. Motility of vinculin-deficient F9 embryonic carcinoma cells analyzed by video, laser confocal, and reflection interference contrast microscopy. Goldmann, W.H., Schindl, M., Cardozo, T.J., Ezzell, R.M. Exp. Cell Res. (1995) [Pubmed]
  14. Genetic analysis of {beta}1 integrin "activation motifs" in mice. Czuchra, A., Meyer, H., Legate, K.R., Brakebusch, C., Fässler, R. J. Cell Biol. (2006) [Pubmed]
  15. Structural basis for phosphatidylinositol phosphate kinase type Igamma binding to talin at focal adhesions. de Pereda, J.M., Wegener, K.L., Santelli, E., Bate, N., Ginsberg, M.H., Critchley, D.R., Campbell, I.D., Liddington, R.C. J. Biol. Chem. (2005) [Pubmed]
  16. An essential role for talin during alpha(M)beta(2)-mediated phagocytosis. Lim, J., Wiedemann, A., Tzircotis, G., Monkley, S.J., Critchley, D.R., Caron, E. Mol. Biol. Cell (2007) [Pubmed]
  17. 1,25-Dihydroxyvitamin D3 and macrophage colony-stimulating factor-1 synergistically phosphorylate talin. Meenakshi, T., Ross, F.P., Martin, J., Teitelbaum, S.L. J. Cell. Biochem. (1993) [Pubmed]
  18. Cytoskeletal architecture in mouse lung epithelial cells is regulated by protein-kinase C-alpha and calpain II. Dwyer-Nield, L.D., Miller, A.C., Neighbors, B.W., Dinsdale, D., Malkinson, A.M. Am. J. Physiol. (1996) [Pubmed]
  19. A chimeric N-cadherin/beta 1-integrin receptor which localizes to both cell-cell and cell-matrix adhesions. Geiger, B., Salomon, D., Takeichi, M., Hynes, R.O. J. Cell. Sci. (1992) [Pubmed]
  20. Phosphatidylinositol phosphate kinase type Igamma directly associates with and regulates Shp-1 tyrosine phosphatase. Bairstow, S.F., Ling, K., Anderson, R.A. J. Biol. Chem. (2005) [Pubmed]
  21. Cell adhesion strengthening: contributions of adhesive area, integrin binding, and focal adhesion assembly. Gallant, N.D., Michael, K.E., García, A.J. Mol. Biol. Cell (2005) [Pubmed]
  22. Differences in elasticity of vinculin-deficient F9 cells measured by magnetometry and atomic force microscopy. Goldmann, W.H., Galneder, R., Ludwig, M., Xu, W., Adamson, E.D., Wang, N., Ezzell, R.M. Exp. Cell Res. (1998) [Pubmed]
  23. Vav is a regulator of cytoskeletal reorganization mediated by the T-cell receptor. Fischer, K.D., Kong, Y.Y., Nishina, H., Tedford, K., Marengère, L.E., Kozieradzki, I., Sasaki, T., Starr, M., Chan, G., Gardener, S., Nghiem, M.P., Bouchard, D., Barbacid, M., Bernstein, A., Penninger, J.M. Curr. Biol. (1998) [Pubmed]
  24. Quantitative methods for analysis of integrin binding and focal adhesion formation on biomaterial surfaces. Keselowsky, B.G., García, A.J. Biomaterials (2005) [Pubmed]
  25. Expression and function of cell surface extracellular matrix receptors in mouse blastocyst attachment and outgrowth. Sutherland, A.E., Calarco, P.G., Damsky, C.H. J. Cell Biol. (1988) [Pubmed]
  26. The activity of the vinculin binding sites in talin is influenced by the stability of the helical bundles that make up the talin rod. Patel, B., Gingras, A.R., Bobkov, A.A., Fujimoto, L.M., Zhang, M., Liddington, R.C., Mazzeo, D., Emsley, J., Roberts, G.C., Barsukov, I.L., Critchley, D.R. J. Biol. Chem. (2006) [Pubmed]
  27. Mapping and consensus sequence identification for multiple vinculin binding sites within the talin rod. Gingras, A.R., Ziegler, W.H., Frank, R., Barsukov, I.L., Roberts, G.C., Critchley, D.R., Emsley, J. J. Biol. Chem. (2005) [Pubmed]
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