메뉴 건너뛰기




Volumn 18, Issue 12, 2010, Pages 1654-1666

Structural diversity in integrin/talin interactions

Author keywords

[No Author keywords available]

Indexed keywords

BETA3 INTEGRIN; INTEGRIN; INTEGRIN BETA1A; INTEGRIN BETA1D; TALIN; TALIN1; TALIN2; UNCLASSIFIED DRUG;

EID: 78649781976     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2010.09.018     Document Type: Article
Times cited : (77)

References (62)
  • 2
  • 6
    • 0029671374 scopus 로고    scopus 로고
    • Beta 1D integrin displaces the beta 1A isoform in striated muscles: Localization at junctional structures and signaling potential in nonmuscle cells
    • A.M. Belkin, N.I. Zhidkova, F. Balzac, F. Altruda, D. Tomatis, A. Maier, G. Tarone, V.E. Koteliansky, and K. Burridge Beta 1D integrin displaces the beta 1A isoform in striated muscles: localization at junctional structures and signaling potential in nonmuscle cells J. Cell Biol. 132 1996 211 226
    • (1996) J. Cell Biol. , vol.132 , pp. 211-226
    • Belkin, A.M.1    Zhidkova, N.I.2    Balzac, F.3    Altruda, F.4    Tomatis, D.5    Maier, A.6    Tarone, G.7    Koteliansky, V.E.8    Burridge, K.9
  • 8
    • 44449148944 scopus 로고    scopus 로고
    • The N-terminal domains of talin cooperate with the phosphotyrosine binding-like domain to activate beta1 and beta3 integrins
    • M. Bouaouina, Y. Lad, and D.A. Calderwood The N-terminal domains of talin cooperate with the phosphotyrosine binding-like domain to activate beta1 and beta3 integrins J. Biol. Chem. 283 2008 6118 6125
    • (2008) J. Biol. Chem. , vol.283 , pp. 6118-6125
    • Bouaouina, M.1    Lad, Y.2    Calderwood, D.A.3
  • 9
    • 1442331993 scopus 로고    scopus 로고
    • Integrin activation
    • D.A. Calderwood Integrin activation J. Cell Sci. 117 2004 657 666
    • (2004) J. Cell Sci. , vol.117 , pp. 657-666
    • Calderwood, D.A.1
  • 12
    • 4043057284 scopus 로고    scopus 로고
    • The talin-tail interaction places integrin activation on FERM ground
    • I.D. Campbell, and M.H. Ginsberg The talin-tail interaction places integrin activation on FERM ground Trends Biochem. Sci. 29 2004 429 435
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 429-435
    • Campbell, I.D.1    Ginsberg, M.H.2
  • 13
    • 46749156984 scopus 로고    scopus 로고
    • Progressive myopathy and defects in the maintenance of myotendinous junctions in mice that lack talin 1 in skeletal muscle
    • F.J. Conti, A. Felder, S. Monkley, M. Schwander, M.R. Wood, R. Lieber, D. Critchley, and U. Muller Progressive myopathy and defects in the maintenance of myotendinous junctions in mice that lack talin 1 in skeletal muscle Development 135 2008 2043 2053
    • (2008) Development , vol.135 , pp. 2043-2053
    • Conti, F.J.1    Felder, A.2    Monkley, S.3    Schwander, M.4    Wood, M.R.5    Lieber, R.6    Critchley, D.7    Muller, U.8
  • 14
    • 70350164118 scopus 로고    scopus 로고
    • Talin 1 and 2 are required for myoblast fusion, sarcomere assembly and the maintenance of myotendinous junctions
    • F.J. Conti, S.J. Monkley, M.R. Wood, D.R. Critchley, and U. Muller Talin 1 and 2 are required for myoblast fusion, sarcomere assembly and the maintenance of myotendinous junctions Development 136 2009 3597 3606
    • (2009) Development , vol.136 , pp. 3597-3606
    • Conti, F.J.1    Monkley, S.J.2    Wood, M.R.3    Critchley, D.R.4    Muller, U.5
  • 15
    • 67650288199 scopus 로고    scopus 로고
    • Biochemical and structural properties of the integrin-associated cytoskeletal protein talin
    • D.R. Critchley Biochemical and structural properties of the integrin-associated cytoskeletal protein talin Annu. Rev. Biophys. 38 2009 235 254
    • (2009) Annu. Rev. Biophys. , vol.38 , pp. 235-254
    • Critchley, D.R.1
  • 19
    • 0028979154 scopus 로고
    • Consequences of lack of beta 1 integrin gene expression in mice
    • R. Fassler, and M. Meyer Consequences of lack of beta 1 integrin gene expression in mice Genes Dev. 9 1995 1896 1908
    • (1995) Genes Dev. , vol.9 , pp. 1896-1908
    • Fassler, R.1    Meyer, M.2
  • 20
    • 34447503697 scopus 로고    scopus 로고
    • Conformational entropy in molecular recognition by proteins
    • K.K. Frederick, M.S. Marlow, K.G. Valentine, and A.J. Wand Conformational entropy in molecular recognition by proteins Nature 448 2007 325 329
    • (2007) Nature , vol.448 , pp. 325-329
    • Frederick, K.K.1    Marlow, M.S.2    Valentine, K.G.3    Wand, A.J.4
  • 24
    • 41949106260 scopus 로고    scopus 로고
    • Cooperative role of the membrane-proximal and -distal residues of the integrin beta3 cytoplasmic domain in regulation of talin-mediated alpha IIb beta3 activation
    • T. Hato, J. Yamanouchi, T. Tamura, Y. Yakushijin, I. Sakai, and M. Yasukawa Cooperative role of the membrane-proximal and -distal residues of the integrin beta3 cytoplasmic domain in regulation of talin-mediated alpha IIb beta3 activation J. Biol. Chem. 283 2008 5662 5668
    • (2008) J. Biol. Chem. , vol.283 , pp. 5662-5668
    • Hato, T.1    Yamanouchi, J.2    Tamura, T.3    Yakushijin, Y.4    Sakai, I.5    Yasukawa, M.6
  • 27
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • R.O. Hynes Integrins: bidirectional, allosteric signaling machines Cell 110 2002 673 687
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 28
    • 0024449503 scopus 로고
    • Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • L.E. Kay, D.A. Torchia, and A. Bax Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease Biochemistry 28 1989 8972 8979
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 29
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • R. Koradi, M. Billeter, and K. Wuthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graph. 14 1996 51 55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 30
    • 0029662315 scopus 로고    scopus 로고
    • Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: Conformational disorder mediates binding diversity
    • R.W. Kriwacki, L. Hengst, L. Tennant, S.I. Reed, and P.E. Wright Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity Proc. Natl. Acad. Sci. USA 93 1996 11504 11509
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11504-11509
    • Kriwacki, R.W.1    Hengst, L.2    Tennant, L.3    Reed, S.I.4    Wright, P.E.5
  • 31
    • 0033550299 scopus 로고    scopus 로고
    • Salt bridge stability in monomeric proteins
    • S. Kumar, and R. Nussinov Salt bridge stability in monomeric proteins J. Mol. Biol. 293 1999 1241 1255
    • (1999) J. Mol. Biol. , vol.293 , pp. 1241-1255
    • Kumar, S.1    Nussinov, R.2
  • 32
    • 41449108071 scopus 로고    scopus 로고
    • Structure of the integrin beta3 transmembrane segment in phospholipid bicelles and detergent micelles
    • T.L. Lau, A.W. Partridge, M.H. Ginsberg, and T.S. Ulmer Structure of the integrin beta3 transmembrane segment in phospholipid bicelles and detergent micelles Biochemistry 47 2008 4008 4016
    • (2008) Biochemistry , vol.47 , pp. 4008-4016
    • Lau, T.L.1    Partridge, A.W.2    Ginsberg, M.H.3    Ulmer, T.S.4
  • 33
    • 65649127175 scopus 로고    scopus 로고
    • The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling
    • T.L. Lau, C. Kim, M.H. Ginsberg, and T.S. Ulmer The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling EMBO J. 28 2009 1351 1361
    • (2009) EMBO J. , vol.28 , pp. 1351-1361
    • Lau, T.L.1    Kim, C.2    Ginsberg, M.H.3    Ulmer, T.S.4
  • 34
    • 61449213806 scopus 로고    scopus 로고
    • Mechanisms that regulate adaptor binding to beta-integrin cytoplasmic tails
    • K.R. Legate, and R. Fassler Mechanisms that regulate adaptor binding to beta-integrin cytoplasmic tails J. Cell Sci. 122 2009 187 198
    • (2009) J. Cell Sci. , vol.122 , pp. 187-198
    • Legate, K.R.1    Fassler, R.2
  • 35
    • 0037207135 scopus 로고    scopus 로고
    • Characterization of the monomeric form of the transmembrane and cytoplasmic domains of the integrin beta 3 subunit by NMR spectroscopy
    • R. Li, C.R. Babu, K. Valentine, J.D. Lear, A.J. Wand, J.S. Bennett, and W.F. DeGrado Characterization of the monomeric form of the transmembrane and cytoplasmic domains of the integrin beta 3 subunit by NMR spectroscopy Biochemistry 41 2002 15618 15624
    • (2002) Biochemistry , vol.41 , pp. 15618-15624
    • Li, R.1    Babu, C.R.2    Valentine, K.3    Lear, J.D.4    Wand, A.J.5    Bennett, J.S.6    Degrado, W.F.7
  • 36
    • 0033731119 scopus 로고    scopus 로고
    • Integrin cytoplasmic domain-binding proteins
    • S. Liu, D.A. Calderwood, and M.H. Ginsberg Integrin cytoplasmic domain-binding proteins J. Cell Sci. 113 2000 3563 3571
    • (2000) J. Cell Sci. , vol.113 , pp. 3563-3571
    • Liu, S.1    Calderwood, D.A.2    Ginsberg, M.H.3
  • 39
    • 0028447768 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters
    • V. Munoz, and L. Serrano Elucidating the folding problem of helical peptides using empirical parameters Nat. Struct. Biol. 1 1994 399 409
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 399-409
    • Munoz, V.1    Serrano, L.2
  • 41
    • 41949131361 scopus 로고    scopus 로고
    • An integrin phosphorylation switch: The effect of beta3 integrin tail phosphorylation on Dok1 and talin binding
    • C.L. Oxley, N.J. Anthis, E.D. Lowe, I. Vakonakis, I.D. Campbell, and K.L. Wegener An integrin phosphorylation switch: the effect of beta3 integrin tail phosphorylation on Dok1 and talin binding J. Biol. Chem. 283 2008 5420 5426
    • (2008) J. Biol. Chem. , vol.283 , pp. 5420-5426
    • Oxley, C.L.1    Anthis, N.J.2    Lowe, E.D.3    Vakonakis, I.4    Campbell, I.D.5    Wegener, K.L.6
  • 42
    • 0030059689 scopus 로고    scopus 로고
    • Forces contributing to the conformational stability of proteins
    • C.N. Pace, B.A. Shirley, M. McNutt, and K. Gajiwala Forces contributing to the conformational stability of proteins FASEB J. 10 1996 75 83
    • (1996) FASEB J. , vol.10 , pp. 75-83
    • Pace, C.N.1    Shirley, B.A.2    McNutt, M.3    Gajiwala, K.4
  • 44
    • 33847217997 scopus 로고    scopus 로고
    • Talin2 is induced during striated muscle differentiation and is targeted to stable adhesion complexes in mature muscle
    • M.A. Senetar, C.L. Moncman, and R.O. McCann Talin2 is induced during striated muscle differentiation and is targeted to stable adhesion complexes in mature muscle Cell Motil. Cytoskeleton 64 2007 157 173
    • (2007) Cell Motil. Cytoskeleton , vol.64 , pp. 157-173
    • Senetar, M.A.1    Moncman, C.L.2    McCann, R.O.3
  • 47
    • 65249102824 scopus 로고    scopus 로고
    • Close encounters of the third kind: Disordered domains and the interactions of proteins
    • P. Tompa, M. Fuxreiter, C.J. Oldfield, I. Simon, A.K. Dunker, and V.N. Uversky Close encounters of the third kind: disordered domains and the interactions of proteins Bioessays 31 2009 328 335
    • (2009) Bioessays , vol.31 , pp. 328-335
    • Tompa, P.1    Fuxreiter, M.2    Oldfield, C.J.3    Simon, I.4    Dunker, A.K.5    Uversky, V.N.6
  • 48
    • 0035954396 scopus 로고    scopus 로고
    • NMR analysis of structure and dynamics of the cytosolic tails of integrin alpha IIb beta 3 in aqueous solution
    • T.S. Ulmer, B. Yaspan, M.H. Ginsberg, and I.D. Campbell NMR analysis of structure and dynamics of the cytosolic tails of integrin alpha IIb beta 3 in aqueous solution Biochemistry 40 2001 7498 7508
    • (2001) Biochemistry , vol.40 , pp. 7498-7508
    • Ulmer, T.S.1    Yaspan, B.2    Ginsberg, M.H.3    Campbell, I.D.4
  • 49
    • 0037031551 scopus 로고    scopus 로고
    • A structural mechanism of integrin alpha(IIb)beta(3) "inside- out" activation as regulated by its cytoplasmic face
    • O. Vinogradova, A. Velyvis, A. Velyviene, B. Hu, T. Haas, E. Plow, and J. Qin A structural mechanism of integrin alpha(IIb)beta(3) "inside-out" activation as regulated by its cytoplasmic face Cell 110 2002 587 597
    • (2002) Cell , vol.110 , pp. 587-597
    • Vinogradova, O.1    Velyvis, A.2    Velyviene, A.3    Hu, B.4    Haas, T.5    Plow, E.6    Qin, J.7
  • 50
  • 52
    • 49349085136 scopus 로고    scopus 로고
    • Structural basis for the interaction between the cytoplasmic domain of the hyaluronate receptor layilin and the talin F3 subdomain
    • K.L. Wegener, J. Basran, C.R. Bagshaw, I.D. Campbell, G.C. Roberts, D.R. Critchley, and I.L. Barsukov Structural basis for the interaction between the cytoplasmic domain of the hyaluronate receptor layilin and the talin F3 subdomain J. Mol. Biol. 382 2008 112 126
    • (2008) J. Mol. Biol. , vol.382 , pp. 112-126
    • Wegener, K.L.1    Basran, J.2    Bagshaw, C.R.3    Campbell, I.D.4    Roberts, G.C.5    Critchley, D.R.6    Barsukov, I.L.7
  • 53
    • 0037197990 scopus 로고    scopus 로고
    • Solution structures of the cytoplasmic tail complex from platelet integrin alpha IIb- and beta 3-subunits
    • A.M. Weljie, P.M. Hwang, and H.J. Vogel Solution structures of the cytoplasmic tail complex from platelet integrin alpha IIb- and beta 3-subunits Proc. Natl. Acad. Sci. USA 99 2002 5878 5883
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5878-5883
    • Weljie, A.M.1    Hwang, P.M.2    Vogel, H.J.3
  • 54
    • 0030005250 scopus 로고    scopus 로고
    • Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides
    • W.C. Wimley, T.P. Creamer, and S.H. White Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides Biochemistry 35 1996 5109 5124
    • (1996) Biochemistry , vol.35 , pp. 5109-5124
    • Wimley, W.C.1    Creamer, T.P.2    White, S.H.3
  • 56
    • 76349099822 scopus 로고    scopus 로고
    • Structure of an integrin with an alphaI domain, complement receptor type 4
    • C. Xie, J. Zhu, X. Chen, L. Mi, N. Nishida, and T.A. Springer Structure of an integrin with an alphaI domain, complement receptor type 4 EMBO J. 29 2010 666 679
    • (2010) EMBO J. , vol.29 , pp. 666-679
    • Xie, C.1    Zhu, J.2    Chen, X.3    Mi, L.4    Nishida, N.5    Springer, T.A.6
  • 58
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand
    • J.P. Xiong, T. Stehle, R. Zhang, A. Joachimiak, M. Frech, S.L. Goodman, and M.A. Arnaout Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand Science 296 2002 151 155
    • (2002) Science , vol.296 , pp. 151-155
    • Xiong, J.P.1    Stehle, T.2    Zhang, R.3    Joachimiak, A.4    Frech, M.5    Goodman, S.L.6    Arnaout, M.A.7
  • 59
    • 4644272216 scopus 로고    scopus 로고
    • A novel adaptation of the integrin PSI domain revealed from its crystal structure
    • J.P. Xiong, T. Stehle, S.L. Goodman, and M.A. Arnaout A novel adaptation of the integrin PSI domain revealed from its crystal structure J. Biol. Chem. 279 2004 40252 40254
    • (2004) J. Biol. Chem. , vol.279 , pp. 40252-40254
    • Xiong, J.P.1    Stehle, T.2    Goodman, S.L.3    Arnaout, M.A.4
  • 61
    • 70449566822 scopus 로고    scopus 로고
    • Structure of an integrin alphaIIb beta3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation
    • J. Yang, Y.Q. Ma, R.C. Page, S. Misra, E.F. Plow, and J. Qin Structure of an integrin alphaIIb beta3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation Proc. Natl. Acad. Sci. USA 106 2009 17729 17734
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 17729-17734
    • Yang, J.1    Ma, Y.Q.2    Page, R.C.3    Misra, S.4    Plow, E.F.5    Qin, J.6
  • 62
    • 57749116060 scopus 로고    scopus 로고
    • Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces
    • J. Zhu, B.H. Luo, T. Xiao, C. Zhang, N. Nishida, and T.A. Springer Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces Mol. Cell 32 2008 849 861
    • (2008) Mol. Cell , vol.32 , pp. 849-861
    • Zhu, J.1    Luo, B.H.2    Xiao, T.3    Zhang, C.4    Nishida, N.5    Springer, T.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.