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Gene Review

TLN1  -  talin 1

Gallus gallus

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Disease relevance of TLN1


High impact information on TLN1


Chemical compound and disease context of TLN1

  • The phosphorylation of talin on tyrosine may be crucial for the expression of the abnormal morphology characteristic of cells transformed by Rous sarcoma virus [1].
  • No differences were found in capping efficiency, talin and actin co-localisation or cytoskeletal association of surface-modulated integrin in Rous sarcoma virus (RSV)-transformed cells compared with untransformed counterparts, although differences in the response to cytochalasins were observed [8].

Biological context of TLN1

  • We have found that talin phosphorylation increases 3.0-fold upon exposure of chicken embryo fibroblasts to the tumor-promoting phorbol ester, phorbol 12-myristate 13-acetate [9].
  • Identification of a talin binding site in the cytoskeletal protein vinculin [10].
  • Electron micrographs revealed that the biochemically defined 50-kDa N-terminal talin head domain is composed of two globular subunits, while chemical cross-linking provided evidence that the C-terminal 220-kDa fragment is solely responsible for dimerization [11].
  • Living epithelial cells (PtK2) were microinjected during interphase with fluorescent talin [12].
  • Vinculin and talin: kinetics of entry and exit from the cytoskeletal pool [13].

Anatomical context of TLN1

  • The localization of vinculin and talin in embryonic chicken gizzards indicated that both are primarily cytoplasmic during the first 2 embryonic weeks [14].
  • We discuss the possible roles of vinculin and talin in the assembly of membrane-bound dense plaques during the different phases of smooth-muscle development [14].
  • Only around days 16-18 does talin apparently become associated with the plasma membrane, this being concomitant with the appearance of distinct myofilament-bound dense plaques [14].
  • Immunofluorescence and immunoelectron-microscopic labeling revealed that both proteins are associated with membrane-bound dense plaques in muscle cells; however, the most intense labeling for vinculin was located rather closer to the membrane than that for talin [14].
  • Exposure of the cells to tumor promoter did, however, result in a loss of actin and talin-rich cell surface elaborations that resemble focal contact precursor structures [9].

Associations of TLN1 with chemical compounds


Physical interactions of TLN1

  • The v-src and activated c-src kinases were targeted to adhesion plaques by fusion to the talin-binding sequence of vinculin [16].
  • Normal cells also rapidly formed aggregates of integrin and talin after binding to immobilized fibronectin in a manner that was similar to the transformed cells, suggesting that the aggregation process is not dependent upon activity of the pp60v-src tyrosine kinase [17].
  • Under these conditions dystrophin bound talin with high affinity (Kd 3.5 nM) [18].
  • N-terminal myosin-binding fragment of talin [19].

Co-localisations of TLN1


Regulatory relationships of TLN1


Other interactions of TLN1

  • All of the major components of focal adhesions are also present: alpha-actinin, vinculin, talin, and integrin [22].
  • Within 10 min after binding of cells and fibronectin beads at 22 degrees C or 37 degrees C, integrin and talin aggregated at the membrane adjacent to the site of bead attachment [17].
  • The interaction of dystrophin with purified talin from chicken gizzard was tested by solid phase immunoassay [18].
  • The FERM (four point one, ezrin, radixin, and moesin) domain of talin engages integrins via a novel variant of the canonical phosphotyrosine binding (PTB) domain-NPxY ligand interaction that may be a prototype for FERM domain recognition of transmembrane receptors [7].
  • The position of the actin-binding site at the C terminal suggests that talin may work as a crosslinker between myosin and actin [19].

Analytical, diagnostic and therapeutic context of TLN1


  1. Talin is phosphorylated on tyrosine in chicken embryo fibroblasts transformed by Rous sarcoma virus. Pasquale, E.B., Maher, P.A., Singer, S.J. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  2. Purification of a 190 kDa protein from smooth muscle: relationship to talin. O'Halloran, T., Burridge, K. Biochim. Biophys. Acta (1986) [Pubmed]
  3. Phosphorylation of talin at tyrosine in Rous sarcoma virus-transformed cells. DeClue, J.E., Martin, G.S. Mol. Cell. Biol. (1987) [Pubmed]
  4. Molecular characterization of human tensin. Chen, H., Ishii, A., Wong, W.K., Chen, L.B., Lo, S.H. Biochem. J. (2000) [Pubmed]
  5. Interaction of plasma membrane fibronectin receptor with talin--a transmembrane linkage. Horwitz, A., Duggan, K., Buck, C., Beckerle, M.C., Burridge, K. Nature (1986) [Pubmed]
  6. An interaction between vinculin and talin. Burridge, K., Mangeat, P. Nature (1984) [Pubmed]
  7. Structural determinants of integrin recognition by talin. García-Alvarez, B., de Pereda, J.M., Calderwood, D.A., Ulmer, T.S., Critchley, D., Campbell, I.D., Ginsberg, M.H., Liddington, R.C. Mol. Cell (2003) [Pubmed]
  8. Regulation of integrin mobility and cytoskeletal association in normal and RSV-transformed chick embryo fibroblasts. Horvath, A.R., Kellie, S. J. Cell. Sci. (1990) [Pubmed]
  9. The adhesion plaque protein, talin, is phosphorylated in vivo in chicken embryo fibroblasts exposed to a tumor-promoting phorbol ester. Beckerle, M.C. Cell Regul. (1990) [Pubmed]
  10. Identification of a talin binding site in the cytoskeletal protein vinculin. Jones, P., Jackson, P., Price, G.J., Patel, B., Ohanion, V., Lear, A.L., Critchley, D.R. J. Cell Biol. (1989) [Pubmed]
  11. Energy-filtered electron microscopy reveals that talin is a highly flexible protein composed of a series of globular domains. Winkler, J., Lünsdorf, H., Jockusch, B.M. Eur. J. Biochem. (1997) [Pubmed]
  12. Talin dynamics in living microinjected nonmuscle cells. Hock, R.S., Sanger, J.M., Sanger, J.W. Cell Motil. Cytoskeleton (1989) [Pubmed]
  13. Vinculin and talin: kinetics of entry and exit from the cytoskeletal pool. Lee, S., Otto, J.J. Cell Motil. Cytoskeleton (1997) [Pubmed]
  14. Spatial and temporal relationships between vinculin and talin in the developing chicken gizzard smooth muscle. Volberg, T., Sabanay, H., Geiger, B. Differentiation (1986) [Pubmed]
  15. Identification and localization of talin in chick retinal pigment epithelial cells. Philp, N.J., Yoon, M.Y., Hock, R.S. Exp. Eye Res. (1990) [Pubmed]
  16. Intracellular targeting of pp60src expression: localization of v-src to adhesion plaques is sufficient to transform chicken embryo fibroblasts. Liebl, E.C., Martin, G.S. Oncogene (1992) [Pubmed]
  17. Dynamic cytoskeleton-integrin associations induced by cell binding to immobilized fibronectin. Mueller, S.C., Kelly, T., Dai, M.Z., Dai, H.N., Chen, W.T. J. Cell Biol. (1989) [Pubmed]
  18. Interaction of dystrophin with cytoskeletal proteins: binding to talin and actin. Senter, L., Luise, M., Presotto, C., Betto, R., Teresi, A., Ceoldo, S., Salviati, G. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  19. N-terminal myosin-binding fragment of talin. Lin, Y., Kishi, H., Nakamura, A., Takagi, T., Kohama, K. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  20. Augmentation of alpha-actinin-induced gelation of actin by talin. Muguruma, M., Matsumura, S., Fukazawa, T. J. Biol. Chem. (1992) [Pubmed]
  21. Domain-specific interactions of talin with the membrane-proximal region of the integrin beta3 subunit. Ulmer, T.S., Calderwood, D.A., Ginsberg, M.H., Campbell, I.D. Biochemistry (2003) [Pubmed]
  22. Identification of cytoskeletal, focal adhesion, and cell adhesion proteins in growth cone particles isolated from developing chick brain. Cypher, C., Letourneau, P.C. J. Neurosci. Res. (1991) [Pubmed]
  23. Disintegration of adhesion plaques in chicken embryo fibroblasts upon Rous sarcoma virus-induced transformation: different dissociation rates for talin and vinculin. Brands, R., de Boer, A., Feltkamp, C.A., Roos, E. Exp. Cell Res. (1990) [Pubmed]
  24. Molecular shape and self-association of vinculin and metavinculin. Molony, L., Burridge, K. J. Cell. Biochem. (1985) [Pubmed]
  25. Molecular heterogeneity of adherens junctions. Geiger, B., Volk, T., Volberg, T. J. Cell Biol. (1985) [Pubmed]
  26. Unique geometry of actin-membrane anchorage sites in avian gizzard smooth muscle cells. Draeger, A., Stelzer, E.H., Herzog, M., Small, J.V. J. Cell. Sci. (1989) [Pubmed]
  27. Talin is a post-synaptic component of the rat neuromuscular junction. Sealock, R., Paschal, B., Beckerle, M., Burridge, K. Exp. Cell Res. (1986) [Pubmed]
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