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Volumn 105, Issue 6, 2013, Pages 1304-1315

On the activation of integrin αiIbβ3: Outside-in and inside-out pathways

Author keywords

[No Author keywords available]

Indexed keywords

ARGINYL-GLYCYL-ASPARTIC ACID; ARGINYLGLYCYLASPARTIC ACID; FIBRINOGEN RECEPTOR; LIGAND; OLIGOPEPTIDE; TALIN;

EID: 84884319266     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.07.055     Document Type: Article
Times cited : (58)

References (63)
  • 1
    • 65649127175 scopus 로고    scopus 로고
    • The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling
    • T.L. Lau, and C. Kim 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    Ulmer, T.S.3
  • 7
    • 84875974786 scopus 로고    scopus 로고
    • Localized lipid packing of transmembrane domains impedes integrin clustering
    • M. Mehrbod, and M.R. Mofrad Localized lipid packing of transmembrane domains impedes integrin clustering PLOS Comput. Biol. 9 2013 e1002948
    • (2013) PLOS Comput. Biol. , vol.9 , pp. 1002948
    • Mehrbod, M.1    Mofrad, M.R.2
  • 8
    • 0037452695 scopus 로고    scopus 로고
    • Cells lying on a bed of microneedles: An approach to isolate mechanical force
    • J.L. Tan, and J. Tien C.S. Chen Cells lying on a bed of microneedles: an approach to isolate mechanical force Proc. Natl. Acad. Sci. USA 100 2003 1484 1489
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1484-1489
    • Tan, J.L.1    Tien, J.2    Chen, C.S.3
  • 9
    • 84878507582 scopus 로고    scopus 로고
    • An agent based model of integrin clustering: Exploring the role of ligand clustering, integrin homo-oligomerization, integrin-ligand affinity, membrane crowdedness and ligand mobility
    • Y. Jamali, T. Jamali, and M.R.K. Mofrad An agent based model of integrin clustering: exploring the role of ligand clustering, integrin homo-oligomerization, integrin-ligand affinity, membrane crowdedness and ligand mobility J. Comp. Phys. 244 2012 264 278
    • (2012) J. Comp. Phys. , vol.244 , pp. 264-278
    • Jamali, Y.1    Jamali, T.2    Mofrad, M.R.K.3
  • 10
    • 77949308494 scopus 로고    scopus 로고
    • RGD-ligand mimetic antagonists of integrin alphaIIbbeta3 paradoxically enhance GPVI-induced human platelet activation
    • M.L. Jones, and M.T. Harper A.W. Poole RGD-ligand mimetic antagonists of integrin alphaIIbbeta3 paradoxically enhance GPVI-induced human platelet activation J. Thromb. Haemost. 8 2010 567 576
    • (2010) J. Thromb. Haemost. , vol.8 , pp. 567-576
    • Jones, M.L.1    Harper, M.T.2    Poole, A.W.3
  • 11
    • 34250768894 scopus 로고    scopus 로고
    • Platelet integrin alpha(IIb)beta(3): Activation mechanisms
    • Y.Q. Ma, J. Qin, and E.F. Plow Platelet integrin alpha(IIb)beta(3): activation mechanisms J. Thromb. Haemost. 5 2007 1345 1352
    • (2007) J. Thromb. Haemost. , vol.5 , pp. 1345-1352
    • Ma, Y.Q.1    Qin, J.2    Plow, E.F.3
  • 12
    • 4444264392 scopus 로고    scopus 로고
    • Integrins: Dynamic scaffolds for adhesion and signaling in platelets
    • S.J. Shattil, and P.J. Newman Integrins: dynamic scaffolds for adhesion and signaling in platelets Blood 104 2004 1606 1615
    • (2004) Blood , vol.104 , pp. 1606-1615
    • Shattil, S.J.1    Newman, P.J.2
  • 13
    • 34147140579 scopus 로고    scopus 로고
    • Structure-function analysis reveals discrete beta3 integrin inside-out and outside-in signaling pathways in platelets
    • Z. Zou, and H. Chen M.L. Kahn Structure-function analysis reveals discrete beta3 integrin inside-out and outside-in signaling pathways in platelets Blood 109 2007 3284 3290
    • (2007) Blood , vol.109 , pp. 3284-3290
    • Zou, Z.1    Chen, H.2    Kahn, M.L.3
  • 14
    • 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, and A. Velyvis 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    Qin, J.3
  • 15
    • 8544259562 scopus 로고    scopus 로고
    • Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics
    • T. Xiao, and J. Takagi T.A. Springer Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics Nature 432 2004 59 67
    • (2004) Nature , vol.432 , pp. 59-67
    • Xiao, T.1    Takagi, J.2    Springer, T.A.3
  • 16
    • 0035850669 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin alpha Vbeta3
    • J.P. Xiong, and T. Stehle M.A. Arnaout Crystal structure of the extracellular segment of integrin alpha Vbeta3 Science 294 2001 339 345
    • (2001) Science , vol.294 , pp. 339-345
    • Xiong, J.P.1    Stehle, T.2    Arnaout, M.A.3
  • 17
    • 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, and T. Stehle 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    Arnaout, M.A.3
  • 18
    • 50249106884 scopus 로고    scopus 로고
    • Structural basis for distinctive recognition of fibrinogen gammaC peptide by the platelet integrin alphaIIbbeta3
    • T.A. Springer, J. Zhu, and T. Xiao Structural basis for distinctive recognition of fibrinogen gammaC peptide by the platelet integrin alphaIIbbeta3 J. Cell Biol. 182 2008 791 800
    • (2008) J. Cell Biol. , vol.182 , pp. 791-800
    • Springer, T.A.1    Zhu, J.2    Xiao, T.3
  • 19
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling
    • J. Takagi, and B.M. Petre T.A. Springer Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling Cell 110 2002 599 611
    • (2002) Cell , vol.110 , pp. 599-611
    • Takagi, J.1    Petre, B.M.2    Springer, T.A.3
  • 20
    • 0028077510 scopus 로고
    • Ligand and cation binding are dual functions of a discrete segment of the integrin beta 3 subunit: Cation displacement is involved in ligand binding
    • S.E. D'Souza, and T.A. Haas J.W. Smith Ligand and cation binding are dual functions of a discrete segment of the integrin beta 3 subunit: cation displacement is involved in ligand binding Cell 79 1994 659 667
    • (1994) Cell , vol.79 , pp. 659-667
    • D'Souza, S.E.1    Haas, T.A.2    Smith, J.W.3
  • 22
    • 34249685565 scopus 로고    scopus 로고
    • Tests of the extension and deadbolt models of integrin activation
    • J. Zhu, and B. Boylan T.A. Springer Tests of the extension and deadbolt models of integrin activation J. Biol. Chem. 282 2007 11914 11920
    • (2007) J. Biol. Chem. , vol.282 , pp. 11914-11920
    • Zhu, J.1    Boylan, B.2    Springer, T.A.3
  • 23
    • 0042739086 scopus 로고    scopus 로고
    • New insights into the structural basis of integrin activation
    • J.P. Xiong, and T. Stehle M.A. Arnaout New insights into the structural basis of integrin activation Blood 102 2003 1155 1159
    • (2003) Blood , vol.102 , pp. 1155-1159
    • Xiong, J.P.1    Stehle, T.2    Arnaout, M.A.3
  • 24
    • 0036220127 scopus 로고    scopus 로고
    • Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation
    • N. Beglova, and S.C. Blacklow T.A. Springer Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation Nat. Struct. Biol. 9 2002 282 287
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 282-287
    • Beglova, N.1    Blacklow, S.C.2    Springer, T.A.3
  • 25
    • 9944231967 scopus 로고    scopus 로고
    • Conversion between three conformational states of integrin i domains with a C-terminal pull spring studied with molecular dynamics
    • M. Jin, I. Andricioaei, and T.A. Springer Conversion between three conformational states of integrin I domains with a C-terminal pull spring studied with molecular dynamics Structure 12 2004 2137 2147
    • (2004) Structure , vol.12 , pp. 2137-2147
    • Jin, M.1    Andricioaei, I.2    Springer, T.A.3
  • 29
    • 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, and B.H. Luo 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    Springer, T.A.3
  • 32
    • 0035871686 scopus 로고    scopus 로고
    • A fast SHAKE: Algorithm to solve distance constraint equations for small molecules in molecular dynamics simulations
    • V. Krautler, W.F. Van Gunsteren, and P.H. Hunenberger A fast SHAKE: Algorithm to solve distance constraint equations for small molecules in molecular dynamics simulations J. Comput. Chem. 22 2001 501 508
    • (2001) J. Comput. Chem. , vol.22 , pp. 501-508
    • Krautler, V.1    Van Gunsteren, W.F.2    Hunenberger, P.H.3
  • 33
    • 33845987101 scopus 로고    scopus 로고
    • Structural basis of integrin activation by talin
    • K.L. Wegener, and A.W. Partridge I.D. Campbell Structural basis of integrin activation by talin Cell 128 2007 171 182
    • (2007) Cell , vol.128 , pp. 171-182
    • Wegener, K.L.1    Partridge, A.W.2    Campbell, I.D.3
  • 34
    • 0141865705 scopus 로고    scopus 로고
    • Talin binding to integrin beta tails: A final common step in integrin activation
    • S. Tadokoro, and S.J. Shattil D.A. Calderwood Talin binding to integrin beta tails: a final common step in integrin activation Science 302 2003 103 106
    • (2003) Science , vol.302 , pp. 103-106
    • Tadokoro, S.1    Shattil, S.J.2    Calderwood, D.A.3
  • 35
    • 70449566822 scopus 로고    scopus 로고
    • Structure of an integrin alphaIIb beta3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation
    • J. Yang, and Y.Q. Ma 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    Qin, J.3
  • 36
    • 77957779535 scopus 로고    scopus 로고
    • The Structure of the talin head reveals a novel extended conformation of the FERM domain
    • P.R. Elliott, and B.T. Goult I.L. Barsukov The Structure of the talin head reveals a novel extended conformation of the FERM domain Structure 18 2010 1289 1299
    • (2010) Structure , vol.18 , pp. 1289-1299
    • Elliott, P.R.1    Goult, B.T.2    Barsukov, I.L.3
  • 39
    • 0036902235 scopus 로고    scopus 로고
    • Close-range electrostatic interactions in proteins
    • S. Kumar, and R. Nussinov Close-range electrostatic interactions in proteins ChemBioChem 3 2002 604 617
    • (2002) ChemBioChem , vol.3 , pp. 604-617
    • Kumar, S.1    Nussinov, R.2
  • 41
    • 50449098285 scopus 로고    scopus 로고
    • Mechanisms of thrombus formation
    • B. Furie, and B.C. Furie Mechanisms of thrombus formation N. Engl. J. Med. 359 2008 938 949
    • (2008) N. Engl. J. Med. , vol.359 , pp. 938-949
    • Furie, B.1    Furie, B.C.2
  • 42
    • 0032101012 scopus 로고    scopus 로고
    • RhoA and the function of platelet integrin alphaIIbbeta3
    • L.J. Leng, and H. Kashiwagi S.J. Shattil RhoA and the function of platelet integrin alphaIIbbeta3 Blood 91 1998 4206 4215
    • (1998) Blood , vol.91 , pp. 4206-4215
    • Leng, L.J.1    Kashiwagi, H.2    Shattil, S.J.3
  • 43
    • 67049146466 scopus 로고    scopus 로고
    • Molecular mechanics of the alpha-actinin rod domain: Bending, torsional, and extensional behavior
    • J. Golji, R. Collins, and M.R. Mofrad Molecular mechanics of the alpha-actinin rod domain: bending, torsional, and extensional behavior PLOS Comput. Biol. 5 2009 e1000389
    • (2009) PLOS Comput. Biol. , vol.5 , pp. 1000389
    • Golji, J.1    Collins, R.2    Mofrad, M.R.3
  • 44
    • 78751692682 scopus 로고    scopus 로고
    • Vinculin activation is necessary for complete talin binding
    • J. Golji, J. Lam, and M.R. Mofrad Vinculin activation is necessary for complete talin binding Biophys. J. 100 2011 332 340
    • (2011) Biophys. J. , vol.100 , pp. 332-340
    • Golji, J.1    Lam, J.2    Mofrad, M.R.3
  • 45
    • 77958171400 scopus 로고    scopus 로고
    • A molecular dynamics investigation of vinculin activation
    • J. Golji, and M.R. Mofrad A molecular dynamics investigation of vinculin activation Biophys. J. 99 2010 1073 1081
    • (2010) Biophys. J. , vol.99 , pp. 1073-1081
    • Golji, J.1    Mofrad, M.R.2
  • 46
    • 84860475799 scopus 로고    scopus 로고
    • Phosphorylation primes vinculin for activation
    • J. Golji, T. Wendorff, and M.R. Mofrad Phosphorylation primes vinculin for activation Biophys. J. 102 2012 2022 2030
    • (2012) Biophys. J. , vol.102 , pp. 2022-2030
    • Golji, J.1    Wendorff, T.2    Mofrad, M.R.3
  • 47
    • 84869408749 scopus 로고    scopus 로고
    • A molecular trajectory of α-actinin activation
    • H. Shams, J. Golji, and M.R. Mofrad A molecular trajectory of α-actinin activation Biophys. J. 103 2012 2050 2059
    • (2012) Biophys. J. , vol.103 , pp. 2050-2059
    • Shams, H.1    Golji, J.2    Mofrad, M.R.3
  • 48
    • 33644815614 scopus 로고    scopus 로고
    • Force-induced unfolding of the focal adhesion targeting domain and the influence of paxillin binding
    • M.R. Mofrad, and J. Golji R.D. Kamm Force-induced unfolding of the focal adhesion targeting domain and the influence of paxillin binding Mech. Chem. Biosyst. 1 2004 253 265
    • (2004) Mech. Chem. Biosyst. , vol.1 , pp. 253-265
    • Mofrad, M.R.1    Golji, J.2    Kamm, R.D.3
  • 49
    • 84876908782 scopus 로고    scopus 로고
    • The interaction of vinculin with actin
    • J. Golji, and M.R. Mofrad The interaction of vinculin with actin PLOS Comput. Biol. 9 2013 e1002995
    • (2013) PLOS Comput. Biol. , vol.9
    • Golji, J.1    Mofrad, M.R.2
  • 50
    • 0032820710 scopus 로고    scopus 로고
    • Integrin alpha(IIb)beta(3) signaling in platelet adhesion and aggregation
    • L.V. Parise Integrin alpha(IIb)beta(3) signaling in platelet adhesion and aggregation Curr. Opin. Cell Biol. 11 1999 597 601
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 597-601
    • Parise, L.V.1
  • 51
    • 0032523064 scopus 로고    scopus 로고
    • Integrin signaling: The platelet paradigm
    • S.J. Shattil, H. Kashiwagi, and N. Pampori Integrin signaling: the platelet paradigm Blood 91 1998 2645 2657
    • (1998) Blood , vol.91 , pp. 2645-2657
    • Shattil, S.J.1    Kashiwagi, H.2    Pampori, N.3
  • 52
    • 0037195164 scopus 로고    scopus 로고
    • Three-dimensional model of the human platelet integrin alpha IIbbeta 3 based on electron cryomicroscopy and x-ray crystallography
    • B.D. Adair, and M. Yeager Three-dimensional model of the human platelet integrin alpha IIbbeta 3 based on electron cryomicroscopy and x-ray crystallography Proc. Natl. Acad. Sci. USA 99 2002 14059 14064
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14059-14064
    • Adair, B.D.1    Yeager, M.2
  • 54
    • 0033517796 scopus 로고    scopus 로고
    • Effects of ligand-mimetic peptides Arg-Gly-Asp-X (X = Phe, Trp, Ser) on alphaIIbbeta3 integrin conformation and oligomerization
    • R.R. Hantgan, and C. Paumi J.W. Weisel Effects of ligand-mimetic peptides Arg-Gly-Asp-X (X = Phe, Trp, Ser) on alphaIIbbeta3 integrin conformation and oligomerization Biochemistry 38 1999 14461 14474
    • (1999) Biochemistry , vol.38 , pp. 14461-14474
    • Hantgan, R.R.1    Paumi, C.2    Weisel, J.W.3
  • 55
    • 0031569914 scopus 로고    scopus 로고
    • Cell adhesion in vascular biology. New insights into integrin-ligand interaction
    • J.C. Loftus, and R.C. Liddington Cell adhesion in vascular biology. New insights into integrin-ligand interaction J. Clin. Invest. 99 1997 2302 2306
    • (1997) J. Clin. Invest. , vol.99 , pp. 2302-2306
    • Loftus, J.C.1    Liddington, R.C.2
  • 56
    • 70449522914 scopus 로고    scopus 로고
    • Predicting ligand binding affinity with alchemical free energy methods in a polar model binding site
    • S.E. Boyce, and D.L. Mobley B.K. Shoichet Predicting ligand binding affinity with alchemical free energy methods in a polar model binding site J. Mol. Biol. 394 2009 747 763
    • (2009) J. Mol. Biol. , vol.394 , pp. 747-763
    • Boyce, S.E.1    Mobley, D.L.2    Shoichet, B.K.3
  • 58
    • 0035941265 scopus 로고    scopus 로고
    • Amino acid residues in the alpha IIb subunit that are critical for ligand binding to integrin alpha IIbbeta 3 are clustered in the beta-propeller model
    • T. Kamata, and K.K. Tieu Y. Takada Amino acid residues in the alpha IIb subunit that are critical for ligand binding to integrin alpha IIbbeta 3 are clustered in the beta-propeller model J. Biol. Chem. 276 2001 44275 44283
    • (2001) J. Biol. Chem. , vol.276 , pp. 44275-44283
    • Kamata, T.1    Tieu, K.K.2    Takada, Y.3
  • 59
    • 0035041854 scopus 로고    scopus 로고
    • C-terminal opening mimics 'inside-out' activation of integrin alpha5beta1
    • J. Takagi, H.P. Erickson, and T.A. Springer C-terminal opening mimics 'inside-out' activation of integrin alpha5beta1 Nat. Struct. Biol. 8 2001 412 416
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 412-416
    • Takagi, J.1    Erickson, H.P.2    Springer, T.A.3
  • 60
    • 0037131270 scopus 로고    scopus 로고
    • Agonist-specific structural rearrangements of integrin alpha IIbbeta 3. Confirmation of the bent conformation in platelets at rest and after activation
    • M.J. Calzada, M.V. Alvarez, and J. Gonzalez-Rodriguez Agonist-specific structural rearrangements of integrin alpha IIbbeta 3. Confirmation of the bent conformation in platelets at rest and after activation J. Biol. Chem. 277 2002 39899 39908
    • (2002) J. Biol. Chem. , vol.277 , pp. 39899-39908
    • Calzada, M.J.1    Alvarez, M.V.2    Gonzalez-Rodriguez, J.3
  • 61
    • 0033546144 scopus 로고    scopus 로고
    • Peptide ligands can bind to distinct sites in integrin alphaIIbbeta3 and elicit different functional responses
    • C.S. Cierniewski, and T. Byzova E.F. Plow Peptide ligands can bind to distinct sites in integrin alphaIIbbeta3 and elicit different functional responses J. Biol. Chem. 274 1999 16923 16932
    • (1999) J. Biol. Chem. , vol.274 , pp. 16923-16932
    • Cierniewski, C.S.1    Byzova, T.2    Plow, E.F.3
  • 62
    • 0036087390 scopus 로고    scopus 로고
    • Transmembrane signal transduction of the alpha(IIb)beta(3) integrin
    • K.E. Gottschalk, and P.D. Adams H. Kessler Transmembrane signal transduction of the alpha(IIb)beta(3) integrin Protein Sci. 11 2002 1800 1812
    • (2002) Protein Sci. , vol.11 , pp. 1800-1812
    • Gottschalk, K.E.1    Adams, P.D.2    Kessler, H.3
  • 63
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • M. Kim, C.V. Carman, and T.A. Springer Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins Science 301 2003 1720 1725
    • (2003) Science , vol.301 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3


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