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Talin protein



talin 1
Identifiers
Symbol TLN1
Alt. Symbols TLN
Entrez 7094
HUGO 11845
OMIM 186745
RefSeq NM_006289
UniProt Q9Y490
Other data
Locus Chr. 9 p23-p21
talin 2
Identifiers
Symbol TLN2
Entrez 83660
HUGO 15447
OMIM 607349
RefSeq NM_015059
UniProt Q9Y4G6
Other data
Locus Chr. 15 q15-q21


TALIN is a high-molecular-weight cytoskeletal protein concentrated at regions of cell–substratum contact[1] and, in lymphocytes, at cell–cell contacts[2][3]. Talin is a ubiquitous cytosolic protein that is found in high concentrations in focal adhesions. It is capable of linking integrins to the actin cytoskeleton either directly or indirectly by interacting with vinculin and alpha-actinin[4]. Integrin receptors are involved in the attachment of adherent cells to extracellular matrices[5][6] and of lymphocytes to other cells. In these situations, talin codistributes with concentrations of integrins in the cell surface membrane [7][8]. Furthermore, in vitro binding studies suggest that integrins bind to talin, although with low affinity[9]. Talin also binds with high affinity to vinculin[10], another cytoskeletal protein concentrated at points of cell adhesion[11]. Finally, talin is a substrate for the Ca2+-activated protease, calpain II[12], which is also concentrated at points of cell-substratum contact[13].

Additional recommended knowledge

Contents

Talin Domains

Talin consists of a large C-terminal rod domain that contains bundles of α-alpha helices and an N-terminal FERM (band 4.1, ezrin, radixin, and moesin) domain with three subdomains: F1, F2, and F3[14][15][16][17]. The F3 subdomain of the FERM domain contains the highest affinity integrin-binding site for integrin β tails and is sufficient to activate integrins[18].

 

Talin Activates Integrin αIIbβ3

A structure-function analysis reported recently[19] provides a cogent structural model (see top right) to explain talin-dependent integrin activation in three steps:

♦ (A) The talin F3 domain (surface representation; colored by charge), freed from its autoinhibitory interactions in the full-length protein, becomes available for binding to the integrin.
♦ (B) F3 engages the membrane-distal part of the β3-integrin tail (in red), which becomes ordered, but the α-β integrin interactions that hold the integrin in the low-affinity conformation remain intact.
♦ (C) In a subsequent step, F3 engages the membrane-proximal portion of the β3 tail while maintaining its membrane-distal interactions.

References

  1. ^ Burridge, K. & Connell, L. J. Cell Biol. 97, 359−367 (1983)
  2. ^ Kupfer, A., Singer, S. J. & Dennert, G. J. exp. Med. 163, 489−498 (1986)
  3. ^ Burn, P., Kupfer, A. & Singer, S. J. Proc. natn. Acad. Sci. U.S.A. 85, 497−501 (1988)
  4. ^ Michelson, A. D. (2006). Platelets, Academic Press.
  5. ^ Hynes, R. O. Cell 48, 549−554 (1987)
  6. ^ Ruoslahti, E. & Pierschbacher, M. D. Science 238, 491−497 (1987)
  7. ^ Chen, W, T., Hasegawa, T., Hasegawa, C., Weinstock, C. & Yamada, K. M. J. Cell Biol. 100, 1103−1114 (1985)
  8. ^ Kupfer, A. & Singer, S. J. J. exp. Med. 170, 1697−1713 (1989)
  9. ^ Horwitz, A., Duggan, E., Buck, C., Beckerle, M. C. & Burridge, K. Nature 320, 531−533 (1986)
  10. ^ Burridge, K. & Mangeat, P. Nature 308, 744−746 (1984)
  11. ^ Geiger, B. Cell 18, 193−205 (1979)
  12. ^ Fox, J. E. B., Goll, D. E., Reynolds, C. C. & Phillips, D. R. J. biol. Chem. 260, 1060−1066 (1985
  13. ^ Beckerle, M. C., Burridge, K., DeMartino, G. N. & Croall, D. E. Cell 51, 569−577 (1987)
  14. ^ Chishti A.H. et al., Trends Biochem. Sci. 23 (1998), pp. 281–282
  15. ^ Garcia-Alvarez B. et al., Mol. Cell 11 (2003), pp. 49–58.
  16. ^ Papagrigoriou E. et al., EMBO J. 23 (2004), pp. 2942–2951
  17. ^ Rees D.J. et al., Nature 347 (1990), pp. 685–689.
  18. ^ Calderwood D.A. et al., 2002 J. Biol. Chem. 277 (2002), pp. 21749–21758
  19. ^ Wegener, K.L. et al., Cell (2007) 128(1):171-82


See also

 
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Talin_protein". A list of authors is available in Wikipedia.
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