Name= talin 1
TALIN is a high-molecular-weight
cytoskeletalprotein concentrated at regions of cell–substratum contactcite journal | author = Burridge K, Connell L | title = A new protein of adhesion plaques and ruffling membranes | journal = J. Cell Biol. | volume = 97 | issue = 2 | pages = 359–67 | year = 1983 | pmid = 6684120 | doi = 10.1083/jcb.97.2.359 | issn = ] and, in lymphocytes, at cell–cell contacts.cite journal | author = Kupfer A, Singer SJ, Dennert G | title = On the mechanism of unidirectional killing in mixtures of two cytotoxic T lymphocytes. Unidirectional polarization of cytoplasmic organelles and the membrane-associated cytoskeleton in the effector cell | journal = J. Exp. Med. | volume = 163 | issue = 3 | pages = 489–98 | year = 1986 | pmid = 3081676 | doi = 10.1084/jem.163.3.489 | issn = ] cite journal | author = Burn P, Kupfer A, Singer SJ | title = Dynamic membrane-cytoskeletal interactions: specific association of integrin and talin arises in vivo after phorbol ester treatment of peripheral blood lymphocytes | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 85 | issue = 2 | pages = 497–501 | year = 1988 | pmid = 3124107 | doi = 10.1073/pnas.85.2.497 | issn = ] 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 vinculinand alpha-actinin.cite book | author = Alan D. Michelson | title = Platelets, Second Edition | publisher = Academic Press | location = Boston | year = 2006 | pages = | isbn = 0-12-369367-5 | oclc = | doi = ] Integrinreceptors are involved in the attachment of adherent cells to extracellular matricescite journal | author = Hynes RO | title = Integrins: a family of cell surface receptors | journal = Cell | volume = 48 | issue = 4 | pages = 549–54 | year = 1987 | pmid = 3028640 | doi = 10.1016/0092-8674(87)90233-9 | issn = ] cite journal | author = Ruoslahti E, Pierschbacher MD | title = New perspectives in cell adhesion: RGD and integrins | journal = Science | volume = 238 | issue = 4826 | pages = 491–7 | year = 1987 | pmid = 2821619 | doi = 10.1126/science.2821619 | issn = ] and of lymphocytesto other cells. In these situations, talin codistributes with concentrations of integrins in the cell surface membrane.cite journal | author = Chen WT, Hasegawa E, Hasegawa T, Weinstock C, Yamada KM | title = Development of cell surface linkage complexes in cultured fibroblasts | journal = J. Cell Biol. | volume = 100 | issue = 4 | pages = 1103–14 | year = 1985 | pmid = 3884631 | doi = 10.1083/jcb.100.4.1103 | issn = ] cite journal | author = Kupfer A, Singer SJ | title = The specific interaction of helper T cells and antigen-presenting B cells. IV. Membrane and cytoskeletal reorganizations in the bound T cell as a function of antigen dose | journal = J. Exp. Med. | volume = 170 | issue = 5 | pages = 1697–713 | year = 1989 | pmid = 2530300 | doi = 10.1084/jem.170.5.1697 | issn = ] Furthermore, in vitrobinding studies suggest that integrins bind to talin, although with low affinity.cite journal | author = Horwitz A, Duggan K, Buck C, Beckerle MC, Burridge K | title = Interaction of plasma membrane fibronectin receptor with talin--a transmembrane linkage | journal = Nature | volume = 320 | issue = 6062 | pages = 531–3 | year = 1986 | pmid = 2938015 | doi = 10.1038/320531a0 | issn = ] Talin also binds with high affinity to vinculin,cite journal | author = Burridge K, Mangeat P | title = An interaction between vinculin and talin | journal = Nature | volume = 308 | issue = 5961 | pages = 744–6 | year = 1984 | pmid = 6425696 | doi = 10.1038/308744a0 | issn = ] another cytoskeletalprotein concentrated at points of cell adhesion.cite journal | author = Geiger B | title = A 130K protein from chicken gizzard: its localization at the termini of microfilament bundles in cultured chicken cells | journal = Cell | volume = 18 | issue = 1 | pages = 193–205 | year = 1979 | pmid = 574428 | doi = 10.1016/0092-8674(79)90368-4 | issn = ] Finally, talin is a substrate for the Ca2+-activated protease, calpainII,cite journal | author = Fox JE, Goll DE, Reynolds CC, Phillips DR | title = Identification of two proteins (actin-binding protein and P235) that are hydrolyzed by endogenous Ca2+-dependent protease during platelet aggregation | journal = J. Biol. Chem. | volume = 260 | issue = 2 | pages = 1060–6 | year = 1985 | pmid = 2981831 | doi = | issn = | url = http://www.jbc.org/cgi/content/abstract/260/2/1060] which is also concentrated at points of cell-substratum contact.cite journal | author = Beckerle MC, Burridge K, DeMartino GN, Croall DE | title = Colocalization of calcium-dependent protease II and one of its substrates at sites of cell adhesion | journal = Cell | volume = 51 | issue = 4 | pages = 569–77 | year = 1987 | pmid = 2824061 | doi = 10.1016/0092-8674(87)90126-7 | issn = ]
Talin consists of a large
C-terminalrod domain that contains bundles of α- alpha helicesand an N-terminalFERM (band 4.1, ezrin, radixin, and moesin) domain with three subdomains: F1, F2, and F3.cite journal | author = Chishti AH, Kim AC, Marfatia SM, Lutchman M, Hanspal M, Jindal H, Liu SC, Low PS, Rouleau GA, Mohandas N, Chasis JA, Conboy JG, Gascard P, Takakuwa Y, Huang SC, Benz EJ, Bretscher A, Fehon RG, Gusella JF, Ramesh V, Solomon F, Marchesi VT, Tsukita S, Tsukita S, Hoover KB | title = The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane | journal = Trends Biochem. Sci. | volume = 23 | issue = 8 | pages = 281–2 | year = 1998 | pmid = 9757824 | doi = 10.1016/S0968-0004(98)01237-7 | issn = ] cite journal | author = García-Alvarez B, de Pereda JM, Calderwood DA, Ulmer TS, Critchley D, Campbell ID, Ginsberg MH, Liddington RC | title = Structural determinants of integrin recognition by talin | journal = Mol. Cell | volume = 11 | issue = 1 | pages = 49–58 | year = 2003 | pmid = 12535520 | doi = 10.1016/S1097-2765(02)00823-7 | issn = ] cite journal | author = Papagrigoriou E, Gingras AR, Barsukov IL, Bate N, Fillingham IJ, Patel B, Frank R, Ziegler WH, Roberts GC, Critchley DR, Emsley J | title = Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle | journal = EMBO J. | volume = 23 | issue = 15 | pages = 2942–51 | year = 2004 | pmid = 15272303 | doi = 10.1038/sj.emboj.7600285 | issn = ] cite journal | author = Rees DJ, Ades SE, Singer SJ, Hynes RO | title = Sequence and domain structure of talin | journal = Nature | volume = 347 | issue = 6294 | pages = 685–9 | year = 1990 | pmid = 2120593 | doi = 10.1038/347685a0 | issn = ] The F3 subdomain of the FERM domain contains the highest affinity integrin-binding site for integrinβ tails and is sufficient to activate integrins.cite journal | author = Calderwood DA, Yan B, de Pereda JM, Alvarez BG, Fujioka Y, Liddington RC, Ginsberg MH | title = The phosphotyrosine binding-like domain of talin activates integrins | journal = J. Biol. Chem. | volume = 277 | issue = 24 | pages = 21749–58 | year = 2002 | pmid = 11932255 | doi = 10.1074/jbc.M111996200 | issn = ]
Talin Activates Integrin αIIbβ3
A structure-function analysis reported recentlycite journal | author = Wegener KL, Partridge AW, Han J, Pickford AR, Liddington RC, Ginsberg MH, Campbell ID | title = Structural basis of integrin activation by talin | journal = Cell | volume = 128 | issue = 1 | pages = 171–82 | year = 2007 | pmid = 17218263 | doi = 10.1016/j.cell.2006.10.048 | issn = ] provides a cogent structural model (see top right) to explain talin-dependent
integrinactivation 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- integrintail (in red), which becomes ordered, but the α-β integrininteractions that hold the integrinin 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.
Merlin (protein)an acronym for "Moesin-Ezrin-Radixin-Like Protein"
* [http://ca.expasy.org/uniprot/Q9Y490 Talin-1] UniProtKB/Swiss-Prot entry [ [http://ca.expasy.org/uniprot/Q9Y490 Q9Y490]
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