메뉴 건너뛰기




Volumn 19, Issue 5, 2007, Pages 495-507

Structure and mechanics of integrin-based cell adhesion

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA INTEGRIN; BETA INTEGRIN; VITRONECTIN RECEPTOR;

EID: 35648978998     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2007.08.002     Document Type: Review
Times cited : (340)

References (110)
  • 1
    • 0023666065 scopus 로고
    • Integrins: a family of cell surface receptors
    • Hynes R.O. Integrins: a family of cell surface receptors. Cell 48 (1987) 549-554
    • (1987) Cell , vol.48 , pp. 549-554
    • Hynes, R.O.1
  • 2
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk
    • Geiger B., Bershadsky A., Pankov R., and Yamada K.M. Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk. Nat Rev Mol Cell Biol 2 (2001) 793-805
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.M.4
  • 3
    • 0344465841 scopus 로고    scopus 로고
    • Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells
    • Zaidel-Bar R., Ballestrem C., Kam Z., and Geiger B. Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells. J Cell Sci 116 (2003) 4605-4613
    • (2003) J Cell Sci , vol.116 , pp. 4605-4613
    • Zaidel-Bar, R.1    Ballestrem, C.2    Kam, Z.3    Geiger, B.4
  • 4
    • 33645773666 scopus 로고    scopus 로고
    • Local force and geometry sensing regulate cell functions
    • Vogel V., and Sheetz M. Local force and geometry sensing regulate cell functions. Nat Rev Mol Cell Biol 7 (2006) 265-275
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 265-275
    • Vogel, V.1    Sheetz, M.2
  • 5
    • 0027483226 scopus 로고
    • A novel divalent cation-binding site in the A domain of the beta 2 integrin CR3 (CD11b/CD18) is essential for ligand binding
    • Michishita M., Videm V., and Arnaout M.A. A novel divalent cation-binding site in the A domain of the beta 2 integrin CR3 (CD11b/CD18) is essential for ligand binding. Cell 72 (1993) 857-867
    • (1993) Cell , vol.72 , pp. 857-867
    • Michishita, M.1    Videm, V.2    Arnaout, M.A.3
  • 6
    • 0029646107 scopus 로고
    • Two conformations of the integrin A-domain (I-domain): a pathway for activation?
    • Lee J.O., Bankston L.A., Arnaout M.A., and Liddington R.C. Two conformations of the integrin A-domain (I-domain): a pathway for activation?. Structure 3 (1995) 1333-1340
    • (1995) Structure , vol.3 , pp. 1333-1340
    • Lee, J.O.1    Bankston, L.A.2    Arnaout, M.A.3    Liddington, R.C.4
  • 7
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18)
    • Lee J.O., Rieu P., Arnaout M.A., and Liddington R. Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18). Cell 80 (1995) 631-638
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 8
    • 28444497446 scopus 로고    scopus 로고
    • Integrin structure, allostery, and bidirectional signaling
    • Arnaout M.A., Mahalingam B., and Xiong J.P. Integrin structure, allostery, and bidirectional signaling. Annu Rev Cell Dev Biol 21 (2005) 381-410
    • (2005) Annu Rev Cell Dev Biol , vol.21 , pp. 381-410
    • Arnaout, M.A.1    Mahalingam, B.2    Xiong, J.P.3
  • 9
    • 0032517824 scopus 로고    scopus 로고
    • Two functional states of the CD11b A-domain: correlations with key features of two Mn2+-complexed crystal structures
    • Li R., Rieu P., Griffith D.L., Scott D., and Arnaout M.A. Two functional states of the CD11b A-domain: correlations with key features of two Mn2+-complexed crystal structures. J Cell Biol 143 (1998) 1523-1534
    • (1998) J Cell Biol , vol.143 , pp. 1523-1534
    • Li, R.1    Rieu, P.2    Griffith, D.L.3    Scott, D.4    Arnaout, M.A.5
  • 10
    • 0034624058 scopus 로고    scopus 로고
    • An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain
    • Xiong J.P., Li R., Essafi M., Stehle T., and Arnaout M.A. An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain. J Biol Chem 275 (2000) 38762-38767
    • (2000) J Biol Chem , vol.275 , pp. 38762-38767
    • Xiong, J.P.1    Li, R.2    Essafi, M.3    Stehle, T.4    Arnaout, M.A.5
  • 12
    • 0037428080 scopus 로고    scopus 로고
    • Structures of the alphaL I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation
    • Shimaoka M., Xiao T., Liu J.H., Yang Y., Dong Y., Jun C.D., McCormack A., Zhang R., Joachimiak A., Takagi J., et al. Structures of the alphaL I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation. Cell 112 (2003) 99-111
    • (2003) Cell , vol.112 , pp. 99-111
    • Shimaoka, M.1    Xiao, T.2    Liu, J.H.3    Yang, Y.4    Dong, Y.5    Jun, C.D.6    McCormack, A.7    Zhang, R.8    Joachimiak, A.9    Takagi, J.10
  • 14
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand
    • Xiong J.P., Stehle T., Zhang R., Joachimiak A., Frech M., Goodman S.L., and Arnaout M.A. 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
  • 15
    • 4644272216 scopus 로고    scopus 로고
    • A novel adaptation of the integrin PSI domain revealed from its crystal structure
    • Xiong J.P., Stehle T., Goodman S.L., and Arnaout M.A. 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
  • 16
    • 33845922350 scopus 로고    scopus 로고
    • N-glycosylation of the beta-propeller domain of the integrin alpha5 subunit is essential for alpha5beta1 heterodimerization, expression on the cell surface, and its biological function
    • Specific glycosylation sites on α5β1 that regulate dimerization and transport.
    • Isaji T., Sato Y., Zhao Y., Miyoshi E., Wada Y., Taniguchi N., and Gu J. N-glycosylation of the beta-propeller domain of the integrin alpha5 subunit is essential for alpha5beta1 heterodimerization, expression on the cell surface, and its biological function. J Biol Chem 281 (2006) 33258-33267. Specific glycosylation sites on α5β1 that regulate dimerization and transport.
    • (2006) J Biol Chem , vol.281 , pp. 33258-33267
    • Isaji, T.1    Sato, Y.2    Zhao, Y.3    Miyoshi, E.4    Wada, Y.5    Taniguchi, N.6    Gu, J.7
  • 17
    • 34447536855 scopus 로고    scopus 로고
    • Pactolus i-domain: functional switching of the Rossmann fold
    • Sen M., and Legge G.B. Pactolus i-domain: functional switching of the Rossmann fold. Proteins 68 (2007) 626-635
    • (2007) Proteins , vol.68 , pp. 626-635
    • Sen, M.1    Legge, G.B.2
  • 18
    • 34547106059 scopus 로고    scopus 로고
    • Mutation of a conserved asparagine in the I-like domain promotes constitutively active integrins {alpha}Lbeta2 and {alpha}IIbbeta3
    • Cheng M., Foo S.Y., Shi M.L., Tang R.H., Kong L.S., Law S.K., and Tan S.M. Mutation of a conserved asparagine in the I-like domain promotes constitutively active integrins {alpha}Lbeta2 and {alpha}IIbbeta3. J Biol Chem 282 (2007) 18225-18232
    • (2007) J Biol Chem , vol.282 , pp. 18225-18232
    • Cheng, M.1    Foo, S.Y.2    Shi, M.L.3    Tang, R.H.4    Kong, L.S.5    Law, S.K.6    Tan, S.M.7
  • 19
    • 8544259562 scopus 로고    scopus 로고
    • Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics
    • Xiao T., Takagi J., Coller B.S., Wang J.H., and Springer T.A. 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    Coller, B.S.3    Wang, J.H.4    Springer, T.A.5
  • 20
    • 1642305349 scopus 로고    scopus 로고
    • Locking the beta3 integrin I-like domain into high and low affinity conformations with disulfides
    • Luo B.H., Takagi J., and Springer T.A. Locking the beta3 integrin I-like domain into high and low affinity conformations with disulfides. J Biol Chem 279 (2004) 10215-10221
    • (2004) J Biol Chem , vol.279 , pp. 10215-10221
    • Luo, B.H.1    Takagi, J.2    Springer, T.A.3
  • 21
    • 1442306162 scopus 로고    scopus 로고
    • Activation of integrin beta-subunit I-like domains by one-turn C-terminal alpha-helix deletions
    • Yang W., Shimaoka M., Chen J., and Springer T.A. Activation of integrin beta-subunit I-like domains by one-turn C-terminal alpha-helix deletions. Proc Natl Acad Sci USA 101 (2004) 2333-2338
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2333-2338
    • Yang, W.1    Shimaoka, M.2    Chen, J.3    Springer, T.A.4
  • 22
    • 0035956887 scopus 로고    scopus 로고
    • Locking in alternate conformations of the integrin alphaLbeta2 I domain with disulfide bonds reveals functional relationships among integrin domains
    • Lu C., Shimaoka M., Zang Q., Takagi J., and Springer T.A. Locking in alternate conformations of the integrin alphaLbeta2 I domain with disulfide bonds reveals functional relationships among integrin domains. Proc Natl Acad Sci USA 98 (2001) 2393-2398
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2393-2398
    • Lu, C.1    Shimaoka, M.2    Zang, Q.3    Takagi, J.4    Springer, T.A.5
  • 23
    • 33749522074 scopus 로고    scopus 로고
    • Activation of leukocyte beta(2) integrins by conversion from bent to extended conformations
    • Nishida N., Xie C., Shimaoka M., Cheng Y., Walz T., and Springer T.A. Activation of leukocyte beta(2) integrins by conversion from bent to extended conformations. Immunity 25 (2006) 583-594
    • (2006) Immunity , vol.25 , pp. 583-594
    • Nishida, N.1    Xie, C.2    Shimaoka, M.3    Cheng, Y.4    Walz, T.5    Springer, T.A.6
  • 24
    • 0042739086 scopus 로고    scopus 로고
    • New insights into the structural basis of integrin activation
    • Xiong J.P., Stehle T., Goodman S.L., and Arnaout M.A. 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    Goodman, S.L.3    Arnaout, M.A.4
  • 26
    • 34249685565 scopus 로고    scopus 로고
    • Tests of the extension and deadbolt models of integrin activation
    • Zhu J., Boylan B., Luo B.H., Newman P.J., and Springer T.A. 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    Luo, B.H.3    Newman, P.J.4    Springer, T.A.5
  • 27
    • 0037076494 scopus 로고    scopus 로고
    • Does the integrin alphaA domain act as a ligand for its betaA domain?
    • Alonso J.L., Essafi M., Xiong J.P., Stehle T., and Arnaout M.A. Does the integrin alphaA domain act as a ligand for its betaA domain?. Curr Biol 12 (2002) R340-R342
    • (2002) Curr Biol , vol.12
    • Alonso, J.L.1    Essafi, M.2    Xiong, J.P.3    Stehle, T.4    Arnaout, M.A.5
  • 28
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling
    • Takagi J., Petre B.M., Walz T., and Springer T.A. 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    Walz, T.3    Springer, T.A.4
  • 29
    • 0141625303 scopus 로고    scopus 로고
    • Structure of integrin alpha5beta1 in complex with fibronectin
    • Takagi J., Strokovich K., Springer T.A., and Walz T. Structure of integrin alpha5beta1 in complex with fibronectin. EMBO J 22 (2003) 4607-4615
    • (2003) EMBO J , vol.22 , pp. 4607-4615
    • Takagi, J.1    Strokovich, K.2    Springer, T.A.3    Walz, T.4
  • 30
    • 16844381981 scopus 로고    scopus 로고
    • Three-dimensional EM structure of the ectodomain of integrin {alpha}V{beta}3 in a complex with fibronectin
    • Recombinant extracellular domains of αvβ3 as crystallized in reference [13] remain bent when bound to a macromolecular fibronectin fragment. But an increase in angle of 11 ± 4° between the Hybrid and βA domain is seen.
    • Adair B.D., Xiong J.P., Maddock C., Goodman S.L., Arnaout M.A., and Yeager M. Three-dimensional EM structure of the ectodomain of integrin {alpha}V{beta}3 in a complex with fibronectin. J Cell Biol 168 (2005) 1109-1118. Recombinant extracellular domains of αvβ3 as crystallized in reference [13] remain bent when bound to a macromolecular fibronectin fragment. But an increase in angle of 11 ± 4° between the Hybrid and βA domain is seen.
    • (2005) J Cell Biol , vol.168 , pp. 1109-1118
    • Adair, B.D.1    Xiong, J.P.2    Maddock, C.3    Goodman, S.L.4    Arnaout, M.A.5    Yeager, M.6
  • 31
    • 0037195164 scopus 로고    scopus 로고
    • Three-dimensional model of the human platelet integrin alpha IIbbeta 3 based on electron cryomicroscopy and X-ray crystallography
    • TEM study revealing that the transmembrane helices of αIIb and β3 pack closely in situ and that the receptor does not depart the membrane orthogonally. Evidence for a partially bent structure in a context more native than reference [13].
    • Adair B.D., and Yeager M. 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. TEM study revealing that the transmembrane helices of αIIb and β3 pack closely in situ and that the receptor does not depart the membrane orthogonally. Evidence for a partially bent structure in a context more native than reference [13].
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14059-14064
    • Adair, B.D.1    Yeager, M.2
  • 33
    • 33750337536 scopus 로고    scopus 로고
    • How the headpiece hinge angle is opened: new insights into the dynamics of integrin activation
    • •], while questioning the use of bilaterally amputated integrins in structural studies.
    • •], while questioning the use of bilaterally amputated integrins in structural studies.
    • (2006) J Cell Biol , vol.175 , pp. 349-360
    • Puklin-Faucher, E.1    Gao, M.2    Schulten, K.3    Vogel, V.4
  • 34
    • 33748306120 scopus 로고    scopus 로고
    • Integrin structures and conformational signaling
    • Luo B.H., and Springer T.A. Integrin structures and conformational signaling. Curr Opin Cell Biol 18 (2006) 579-586
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 579-586
    • Luo, B.H.1    Springer, T.A.2
  • 35
    • 33646009721 scopus 로고    scopus 로고
    • Structure and function of myosin filaments
    • Craig R., and Woodhead J.L. Structure and function of myosin filaments. Curr Opin Struct Biol 16 (2006) 204-212
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 204-212
    • Craig, R.1    Woodhead, J.L.2
  • 36
    • 0344981532 scopus 로고    scopus 로고
    • FRET detection of cellular alpha4-integrin conformational activation
    • Chigaev A., Buranda T., Dwyer D.C., Prossnitz E.R., and Sklar L.A. FRET detection of cellular alpha4-integrin conformational activation. Biophys J 85 (2003) 3951-3962
    • (2003) Biophys J , vol.85 , pp. 3951-3962
    • Chigaev, A.1    Buranda, T.2    Dwyer, D.C.3    Prossnitz, E.R.4    Sklar, L.A.5
  • 37
    • 34249815827 scopus 로고    scopus 로고
    • Regulation of cell adhesion by affinity and conformational unbending of alpha4beta1 integrin
    • This and the next paper use FRET between a lipophilic membrane acceptor and an α4β1 mimetic to show a change in distance between integrin head and membrane: inactive-to-active 2.5 nm-7.5 nm, that is shorter than the combined length of the Calf domains. Although this is apparently incompatible with a change from a 'folded' to fully 'extended' structures, it is a signal-averaging technique and so equivocal. Interestingly, the FRET signal, and hence the mean distance of binding site from membrane does not change when the receptor affinity is increased using PMA.
    • Chigaev A., Waller A., Zwartz G.J., Buranda T., and Sklar L.A. Regulation of cell adhesion by affinity and conformational unbending of alpha4beta1 integrin. J Immunol 178 (2007) 6828-6839. This and the next paper use FRET between a lipophilic membrane acceptor and an α4β1 mimetic to show a change in distance between integrin head and membrane: inactive-to-active 2.5 nm-7.5 nm, that is shorter than the combined length of the Calf domains. Although this is apparently incompatible with a change from a 'folded' to fully 'extended' structures, it is a signal-averaging technique and so equivocal. Interestingly, the FRET signal, and hence the mean distance of binding site from membrane does not change when the receptor affinity is increased using PMA.
    • (2007) J Immunol , vol.178 , pp. 6828-6839
    • Chigaev, A.1    Waller, A.2    Zwartz, G.J.3    Buranda, T.4    Sklar, L.A.5
  • 38
    • 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
    • Calzada M.J., Alvarez M.V., and Gonzalez-Rodriguez J. 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
  • 39
    • 23144456804 scopus 로고    scopus 로고
    • AFM imaging of ligand binding to platelet integrin alphaIIbbeta3 receptors reconstituted into planar lipid bilayers
    • An initial effort to using new technologies.
    • Hussain M.A., Agnihotri A., and Siedlecki C.A. AFM imaging of ligand binding to platelet integrin alphaIIbbeta3 receptors reconstituted into planar lipid bilayers. Langmuir 21 (2005) 6979-6986. An initial effort to using new technologies.
    • (2005) Langmuir , vol.21 , pp. 6979-6986
    • Hussain, M.A.1    Agnihotri, A.2    Siedlecki, C.A.3
  • 40
    • 0037452771 scopus 로고    scopus 로고
    • Mechanosensation through integrins: cells act locally but think globally
    • Ingber D.E. Mechanosensation through integrins: cells act locally but think globally. Proc Natl Acad Sci USA 100 (2003) 1472-1474
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1472-1474
    • Ingber, D.E.1
  • 42
    • 33845987101 scopus 로고    scopus 로고
    • Structural basis of integrin activation by talin
    • Elegant description of the interaction of talin with the β3 cytoplasmic domain.
    • Wegener K.L., Partridge A.W., Han J., Pickford A.R., Liddington R.C., Ginsberg M.H., and Campbell I.D. Structural basis of integrin activation by talin. Cell 128 (2007) 171-182. Elegant description of the interaction of talin with the β3 cytoplasmic domain.
    • (2007) Cell , vol.128 , pp. 171-182
    • Wegener, K.L.1    Partridge, A.W.2    Han, J.3    Pickford, A.R.4    Liddington, R.C.5    Ginsberg, M.H.6    Campbell, I.D.7
  • 43
    • 34249821363 scopus 로고    scopus 로고
    • Structure of the PTB domain of tensin1 and a model for its recruitment to fibrillar adhesions
    • McCleverty C.J., Lin D.C., and Liddington R.C. Structure of the PTB domain of tensin1 and a model for its recruitment to fibrillar adhesions. Protein Sci 16 (2007) 1223-1229
    • (2007) Protein Sci , vol.16 , pp. 1223-1229
    • McCleverty, C.J.1    Lin, D.C.2    Liddington, R.C.3
  • 47
    • 21744441321 scopus 로고    scopus 로고
    • Structural dynamics of alpha-actinin-vinculin interactions
    • Bois P.R., Borgon R.A., Vonrhein C., and Izard T. Structural dynamics of alpha-actinin-vinculin interactions. Mol Cell Biol 25 (2005) 6112-6122
    • (2005) Mol Cell Biol , vol.25 , pp. 6112-6122
    • Bois, P.R.1    Borgon, R.A.2    Vonrhein, C.3    Izard, T.4
  • 49
    • 31544465231 scopus 로고    scopus 로고
    • The molecular basis of filamin binding to integrins and competition with talin
    • A second elegant study showing that filamin interaction with β7 cytoplasmic domain has different structural consequences from talin interaction. The binding sites partially overlap, and the authors show biochemically that they compete. This reveals a new mechanism of integrin-cytoskeletal regulation.
    • Kiema T., Lad Y., Jiang P., Oxley C.L., Baldassarre M., Wegener K.L., Campbell I.D., Ylanne J., and Calderwood D.A. The molecular basis of filamin binding to integrins and competition with talin. Mol Cell 21 (2006) 337-347. A second elegant study showing that filamin interaction with β7 cytoplasmic domain has different structural consequences from talin interaction. The binding sites partially overlap, and the authors show biochemically that they compete. This reveals a new mechanism of integrin-cytoskeletal regulation.
    • (2006) Mol Cell , vol.21 , pp. 337-347
    • Kiema, T.1    Lad, Y.2    Jiang, P.3    Oxley, C.L.4    Baldassarre, M.5    Wegener, K.L.6    Campbell, I.D.7    Ylanne, J.8    Calderwood, D.A.9
  • 50
  • 52
    • 0041461882 scopus 로고    scopus 로고
    • Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin
    • Jiang G., Giannone G., Critchley D.R., Fukumoto E., and Sheetz M.P. Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin. Nature 424 (2003) 334-337
    • (2003) Nature , vol.424 , pp. 334-337
    • Jiang, G.1    Giannone, G.2    Critchley, D.R.3    Fukumoto, E.4    Sheetz, M.P.5
  • 53
    • 0242361579 scopus 로고    scopus 로고
    • Talin1 is critical for force-dependent reinforcement of initial integrin-cytoskeleton bonds but not tyrosine kinase activation
    • Giannone G., Jiang G., Sutton D.H., Critchley D.R., and Sheetz M.P. Talin1 is critical for force-dependent reinforcement of initial integrin-cytoskeleton bonds but not tyrosine kinase activation. J Cell Biol 163 (2003) 409-419
    • (2003) J Cell Biol , vol.163 , pp. 409-419
    • Giannone, G.1    Jiang, G.2    Sutton, D.H.3    Critchley, D.R.4    Sheetz, M.P.5
  • 57
    • 0035958967 scopus 로고    scopus 로고
    • Calpain cleavage promotes talin binding to the beta 3 integrin cytoplasmic domain
    • Yan B., Calderwood D.A., Yaspan B., and Ginsberg M.H. Calpain cleavage promotes talin binding to the beta 3 integrin cytoplasmic domain. J Biol Chem 276 (2001) 28164-28170
    • (2001) J Biol Chem , vol.276 , pp. 28164-28170
    • Yan, B.1    Calderwood, D.A.2    Yaspan, B.3    Ginsberg, M.H.4
  • 58
    • 0037031551 scopus 로고    scopus 로고
    • A structural mechanism of integrin alpha(IIb)beta(3)" inside-out" activation as regulated by its cytoplasmic face
    • Vinogradova O., Velyvis A., Velyviene A., Hu B., Haas T., Plow E., and Qin J. 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
  • 60
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • Kim M., Carman C.V., and Springer T.A. 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
  • 62
    • 33744829519 scopus 로고    scopus 로고
    • An interaction between integrin and the talin FERM domain mediates integrin activation but not linkage to the cytoskeleton
    • Tanentzapf G., and Brown N.H. An interaction between integrin and the talin FERM domain mediates integrin activation but not linkage to the cytoskeleton. Nat Cell Biol 8 (2006) 601-606
    • (2006) Nat Cell Biol , vol.8 , pp. 601-606
    • Tanentzapf, G.1    Brown, N.H.2
  • 63
    • 34447116981 scopus 로고    scopus 로고
    • The integrin binding site 2 (IBS2) in the talin rod domain is essential for linking integrin beta subunits to the cytoskeleton
    • The sites in the talin tail revealed, which after binding of the talin head domain regulate propagation of the ECM-cytoskeleton signaling path.
    • Moes M., Rodius S., Coleman S.J., Monkley S.J., Goormaghtigh E., Tremuth L., Kox C., van der Holst P.P., Critchley D.R., and Kieffer N. The integrin binding site 2 (IBS2) in the talin rod domain is essential for linking integrin beta subunits to the cytoskeleton. J Biol Chem 282 (2007) 17280-17288. The sites in the talin tail revealed, which after binding of the talin head domain regulate propagation of the ECM-cytoskeleton signaling path.
    • (2007) J Biol Chem , vol.282 , pp. 17280-17288
    • Moes, M.1    Rodius, S.2    Coleman, S.J.3    Monkley, S.J.4    Goormaghtigh, E.5    Tremuth, L.6    Kox, C.7    van der Holst, P.P.8    Critchley, D.R.9    Kieffer, N.10
  • 64
    • 27544442354 scopus 로고    scopus 로고
    • The mechanisms and dynamics of (alpha)v(beta)3 integrin clustering in living cells
    • Cluzel C., Saltel F., Lussi J., Paulhe F., Imhof B.A., and Wehrle-Haller B. The mechanisms and dynamics of (alpha)v(beta)3 integrin clustering in living cells. J Cell Biol 171 (2005) 383-392
    • (2005) J Cell Biol , vol.171 , pp. 383-392
    • Cluzel, C.1    Saltel, F.2    Lussi, J.3    Paulhe, F.4    Imhof, B.A.5    Wehrle-Haller, B.6
  • 66
    • 33846030511 scopus 로고    scopus 로고
    • Coincidence of actin filaments and talin is required to activate vinculin
    • Chen H., Choudhury D.M., and Craig S.W. Coincidence of actin filaments and talin is required to activate vinculin. J Biol Chem 281 (2006) 40389-40398
    • (2006) J Biol Chem , vol.281 , pp. 40389-40398
    • Chen, H.1    Choudhury, D.M.2    Craig, S.W.3
  • 67
    • 33646368402 scopus 로고    scopus 로고
    • The vinculin binding sites of talin and alpha-actinin are sufficient to activate vinculin
    • Bois P.R., O'Hara B.P., Nietlispach D., Kirkpatrick J., and Izard T. The vinculin binding sites of talin and alpha-actinin are sufficient to activate vinculin. J Biol Chem 281 (2006) 7228-7236
    • (2006) J Biol Chem , vol.281 , pp. 7228-7236
    • Bois, P.R.1    O'Hara, B.P.2    Nietlispach, D.3    Kirkpatrick, J.4    Izard, T.5
  • 69
    • 4644328892 scopus 로고    scopus 로고
    • Paxillin: adapting to change
    • Brown M.C., and Turner C.E. Paxillin: adapting to change. Physiol Rev 84 (2004) 1315-1339
    • (2004) Physiol Rev , vol.84 , pp. 1315-1339
    • Brown, M.C.1    Turner, C.E.2
  • 70
    • 11244258882 scopus 로고    scopus 로고
    • Focal adhesion kinase: in command and control of cell motility
    • Mitra S.K., Hanson D.A., and Schlaepfer D.D. Focal adhesion kinase: in command and control of cell motility. Nat Rev Mol Cell Biol 6 (2005) 56-68
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 56-68
    • Mitra, S.K.1    Hanson, D.A.2    Schlaepfer, D.D.3
  • 71
    • 0036118284 scopus 로고    scopus 로고
    • The structural basis of localization and signaling by the focal adhesion targeting domain
    • Arold S.T., Hoellerer M.K., and Noble M.E. The structural basis of localization and signaling by the focal adhesion targeting domain. Structure 10 (2002) 319-327
    • (2002) Structure , vol.10 , pp. 319-327
    • Arold, S.T.1    Hoellerer, M.K.2    Noble, M.E.3
  • 72
    • 0036172186 scopus 로고    scopus 로고
    • The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin
    • Hayashi I., Vuori K., and Liddington R.C. The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin. Nat Struct Biol 9 (2002) 101-106
    • (2002) Nat Struct Biol , vol.9 , pp. 101-106
    • Hayashi, I.1    Vuori, K.2    Liddington, R.C.3
  • 73
    • 34250026140 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of focal adhesion kinase
    • Lietha D., Cai X., Ceccarelli D.F., Li Y., Schaller M.D., and Eck M.J. Structural basis for the autoinhibition of focal adhesion kinase. Cell 129 (2007) 1177-1187
    • (2007) Cell , vol.129 , pp. 1177-1187
    • Lietha, D.1    Cai, X.2    Ceccarelli, D.F.3    Li, Y.4    Schaller, M.D.5    Eck, M.J.6
  • 74
    • 33751335857 scopus 로고    scopus 로고
    • Force sensing by mechanical extension of the Src family kinase substrate p130Cas
    • A nice study that identifies p130Cas as a primary sensor and transducer of force at focal adhesions.
    • Sawada Y., Tamada M., Dubin-Thaler B.J., Cherniavskaya O., Sakai R., Tanaka S., and Sheetz M.P. Force sensing by mechanical extension of the Src family kinase substrate p130Cas. Cell 127 (2006) 1015-1026. A nice study that identifies p130Cas as a primary sensor and transducer of force at focal adhesions.
    • (2006) Cell , vol.127 , pp. 1015-1026
    • Sawada, Y.1    Tamada, M.2    Dubin-Thaler, B.J.3    Cherniavskaya, O.4    Sakai, R.5    Tanaka, S.6    Sheetz, M.P.7
  • 75
    • 0035954424 scopus 로고    scopus 로고
    • Differential dynamics of alpha 5 integrin, paxillin, and alpha-actinin during formation and disassembly of adhesions in migrating cells
    • Laukaitis C.M., Webb D.J., Donais K., and Horwitz A.F. Differential dynamics of alpha 5 integrin, paxillin, and alpha-actinin during formation and disassembly of adhesions in migrating cells. J Cell Biol 153 (2001) 1427-1440
    • (2001) J Cell Biol , vol.153 , pp. 1427-1440
    • Laukaitis, C.M.1    Webb, D.J.2    Donais, K.3    Horwitz, A.F.4
  • 76
    • 13844253573 scopus 로고    scopus 로고
    • Identification of the beta1-integrin binding site on alpha-actinin by cryoelectron microscopy
    • Kelly D.F., and Taylor K.A. Identification of the beta1-integrin binding site on alpha-actinin by cryoelectron microscopy. J Struct Biol 149 (2005) 290-302
    • (2005) J Struct Biol , vol.149 , pp. 290-302
    • Kelly, D.F.1    Taylor, K.A.2
  • 77
    • 0035823575 scopus 로고    scopus 로고
    • Analysis of the alpha-actinin/zyxin interaction
    • Li B., and Trueb B. Analysis of the alpha-actinin/zyxin interaction. J Biol Chem 276 (2001) 33328-33335
    • (2001) J Biol Chem , vol.276 , pp. 33328-33335
    • Li, B.1    Trueb, B.2
  • 79
    • 0030040067 scopus 로고    scopus 로고
    • Direct binding of the platelet integrin alphaIIbbeta3 (GPIIb-IIIa) to talin. Evidence that interaction is mediated through the cytoplasmic domains of both alphaIIb and beta3
    • Knezevic I., Leisner T.M., and Lam S.C. Direct binding of the platelet integrin alphaIIbbeta3 (GPIIb-IIIa) to talin. Evidence that interaction is mediated through the cytoplasmic domains of both alphaIIb and beta3. J Biol Chem 271 (1996) 16416-16421
    • (1996) J Biol Chem , vol.271 , pp. 16416-16421
    • Knezevic, I.1    Leisner, T.M.2    Lam, S.C.3
  • 80
    • 33748750710 scopus 로고    scopus 로고
    • The interaction between calcium- and integrin-binding protein 1 and the alphaIIb integrin cytoplasmic domain involves a novel C-terminal displacement mechanism
    • Yamniuk A.P., Ishida H., and Vogel H.J. The interaction between calcium- and integrin-binding protein 1 and the alphaIIb integrin cytoplasmic domain involves a novel C-terminal displacement mechanism. J Biol Chem 281 (2006) 26455-26464
    • (2006) J Biol Chem , vol.281 , pp. 26455-26464
    • Yamniuk, A.P.1    Ishida, H.2    Vogel, H.J.3
  • 83
    • 17344366888 scopus 로고    scopus 로고
    • An alpha4 integrin-paxillin-Arf-GAP complex restricts Rac activation to the leading edge of migrating cells
    • Nishiya N., Kiosses W.B., Han J., and Ginsberg M.H. An alpha4 integrin-paxillin-Arf-GAP complex restricts Rac activation to the leading edge of migrating cells. Nat Cell Biol 7 (2005) 343-352
    • (2005) Nat Cell Biol , vol.7 , pp. 343-352
    • Nishiya, N.1    Kiosses, W.B.2    Han, J.3    Ginsberg, M.H.4
  • 84
    • 0042490495 scopus 로고    scopus 로고
    • RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1
    • Katagiri K., Maeda A., Shimonaka M., and Kinashi T. RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1. Nat Immunol 4 (2003) 741-748
    • (2003) Nat Immunol , vol.4 , pp. 741-748
    • Katagiri, K.1    Maeda, A.2    Shimonaka, M.3    Kinashi, T.4
  • 85
    • 12344285901 scopus 로고    scopus 로고
    • Negative regulation of EGFR signalling through integrin-alpha1beta1-mediated activation of protein tyrosine phosphatase TCPTP
    • Mattila E., Pellinen T., Nevo J., Vuoriluoto K., Arjonen A., and Ivaska J. Negative regulation of EGFR signalling through integrin-alpha1beta1-mediated activation of protein tyrosine phosphatase TCPTP. Nat Cell Biol 7 (2005) 78-85
    • (2005) Nat Cell Biol , vol.7 , pp. 78-85
    • Mattila, E.1    Pellinen, T.2    Nevo, J.3    Vuoriluoto, K.4    Arjonen, A.5    Ivaska, J.6
  • 86
    • 33846176546 scopus 로고    scopus 로고
    • Probing the integrin-actin linkage using high-resolution protein velocity mapping
    • ••]) reveal the power of new methodologies in examining motion of structural and regulatory focal-adhesion proteins with actomyosin motors at focal adhesions in live cells.
    • ••]) reveal the power of new methodologies in examining motion of structural and regulatory focal-adhesion proteins with actomyosin motors at focal adhesions in live cells.
    • (2006) J Cell Sci , vol.119 , pp. 5204-5214
    • Brown, C.M.1    Hebert, B.2    Kolin, D.L.3    Zareno, J.4    Whitmore, L.5    Horwitz, A.R.6    Wiseman, P.W.7
  • 87
    • 33846697554 scopus 로고    scopus 로고
    • Differential transmission of actin motion within focal adhesions
    • Hu K., Ji L., Applegate K.T., Danuser G., and Waterman-Storer C.M. Differential transmission of actin motion within focal adhesions. Science 315 (2007) 111-115
    • (2007) Science , vol.315 , pp. 111-115
    • Hu, K.1    Ji, L.2    Applegate, K.T.3    Danuser, G.4    Waterman-Storer, C.M.5
  • 88
    • 34249936024 scopus 로고    scopus 로고
    • Forces and bond dynamics in cell adhesion
    • Evans E.A., and Calderwood D.A. Forces and bond dynamics in cell adhesion. Science 316 (2007) 1148-1153
    • (2007) Science , vol.316 , pp. 1148-1153
    • Evans, E.A.1    Calderwood, D.A.2
  • 89
    • 33646557326 scopus 로고    scopus 로고
    • p130Cas: a versatile scaffold in signaling networks
    • Defilippi P., Di Stefano P., and Cabodi S. p130Cas: a versatile scaffold in signaling networks. Trends Cell Biol 16 (2006) 257-263
    • (2006) Trends Cell Biol , vol.16 , pp. 257-263
    • Defilippi, P.1    Di Stefano, P.2    Cabodi, S.3
  • 91
    • 23844457919 scopus 로고    scopus 로고
    • Specification of the direction of adhesive signaling by the integrin beta cytoplasmic domain
    • Arias-Salgado E.G., Lizano S., Shattil S.J., and Ginsberg M.H. Specification of the direction of adhesive signaling by the integrin beta cytoplasmic domain. J Biol Chem 280 (2005) 29699-29707
    • (2005) J Biol Chem , vol.280 , pp. 29699-29707
    • Arias-Salgado, E.G.1    Lizano, S.2    Shattil, S.J.3    Ginsberg, M.H.4
  • 92
    • 0037437150 scopus 로고    scopus 로고
    • RPTP-alpha acts as a transducer of mechanical force on alphav/beta3-integrin-cytoskeleton linkages
    • von Wichert G., Jiang G., Kostic A., De Vos K., Sap J., and Sheetz M.P. RPTP-alpha acts as a transducer of mechanical force on alphav/beta3-integrin-cytoskeleton linkages. J Cell Biol 161 (2003) 143-153
    • (2003) J Cell Biol , vol.161 , pp. 143-153
    • von Wichert, G.1    Jiang, G.2    Kostic, A.3    De Vos, K.4    Sap, J.5    Sheetz, M.P.6
  • 96
    • 14744281852 scopus 로고    scopus 로고
    • Regulation of the interaction between PIPKI gamma and talin by proline-directed protein kinases
    • Lee S.Y., Voronov S., Letinic K., Nairn A.C., Di Paolo G., and De Camilli P. Regulation of the interaction between PIPKI gamma and talin by proline-directed protein kinases. J Cell Biol 168 (2005) 789-799
    • (2005) J Cell Biol , vol.168 , pp. 789-799
    • Lee, S.Y.1    Voronov, S.2    Letinic, K.3    Nairn, A.C.4    Di Paolo, G.5    De Camilli, P.6
  • 97
    • 0037038412 scopus 로고    scopus 로고
    • Type I gamma phosphatidylinositol phosphate kinase targets and regulates focal adhesions
    • Ling K., Doughman R.L., Firestone A.J., Bunce M.W., and Anderson R.A. Type I gamma phosphatidylinositol phosphate kinase targets and regulates focal adhesions. Nature 420 (2002) 89-93
    • (2002) Nature , vol.420 , pp. 89-93
    • Ling, K.1    Doughman, R.L.2    Firestone, A.J.3    Bunce, M.W.4    Anderson, R.A.5
  • 98
    • 0141865507 scopus 로고    scopus 로고
    • Force-dependent integrin-cytoskeleton linkage formation requires downregulation of focal complex dynamics by Shp2
    • von Wichert G., Haimovich B., Feng G.S., and Sheetz M.P. Force-dependent integrin-cytoskeleton linkage formation requires downregulation of focal complex dynamics by Shp2. EMBO J 22 (2003) 5023-5035
    • (2003) EMBO J , vol.22 , pp. 5023-5035
    • von Wichert, G.1    Haimovich, B.2    Feng, G.S.3    Sheetz, M.P.4
  • 100
    • 33750520931 scopus 로고    scopus 로고
    • Matrix-specific suppression of integrin activation in shear stress signaling
    • Revealing study, which explains how ligation of one integrin can suppress the activation of others: different pathways are activated involving PKA when α2β1 activation suppresses αvβ3, and PKCα when α5β1 suppresses α2β1.
    • Orr A.W., Ginsberg M.H., Shattil S.J., Deckmyn H., and Schwartz M.A. Matrix-specific suppression of integrin activation in shear stress signaling. Mol Biol Cell 17 (2006) 4686-4697. Revealing study, which explains how ligation of one integrin can suppress the activation of others: different pathways are activated involving PKA when α2β1 activation suppresses αvβ3, and PKCα when α5β1 suppresses α2β1.
    • (2006) Mol Biol Cell , vol.17 , pp. 4686-4697
    • Orr, A.W.1    Ginsberg, M.H.2    Shattil, S.J.3    Deckmyn, H.4    Schwartz, M.A.5
  • 102
    • 2442694279 scopus 로고    scopus 로고
    • Determination of N- and C-terminal borders of the transmembrane domain of integrin subunits
    • Stefansson A., Armulik A., Nilsson I., von Heijne G., and Johansson S. Determination of N- and C-terminal borders of the transmembrane domain of integrin subunits. J Biol Chem 279 (2004) 21200-21205
    • (2004) J Biol Chem , vol.279 , pp. 21200-21205
    • Stefansson, A.1    Armulik, A.2    Nilsson, I.3    von Heijne, G.4    Johansson, S.5
  • 103
    • 35648980694 scopus 로고    scopus 로고
    • Transmembrane domain helix packing stabilizes integrin alpha IIbbeta 3 in the low affinity state
    • Partridge A.W., Liu S., Kim S., Bowie J.U., and Ginsberg M.H. Transmembrane domain helix packing stabilizes integrin alpha IIbbeta 3 in the low affinity state. J Biol Chem (2004)
    • (2004) J Biol Chem
    • Partridge, A.W.1    Liu, S.2    Kim, S.3    Bowie, J.U.4    Ginsberg, M.H.5
  • 104
    • 1642529548 scopus 로고    scopus 로고
    • Membrane-mediated structural transitions at the cytoplasmic face during integrin activation
    • Vinogradova O., Vaynberg J., Kong X., Haas T.A., Plow E.F., and Qin J. Membrane-mediated structural transitions at the cytoplasmic face during integrin activation. Proc Natl Acad Sci USA 101 (2004) 4094-4099
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4094-4099
    • Vinogradova, O.1    Vaynberg, J.2    Kong, X.3    Haas, T.A.4    Plow, E.F.5    Qin, J.6
  • 105
    • 18944403970 scopus 로고    scopus 로고
    • A coiled-coil structure of the alphaIIbbeta3 integrin transmembrane and cytoplasmic domains in its resting state
    • Gottschalk K.E. A coiled-coil structure of the alphaIIbbeta3 integrin transmembrane and cytoplasmic domains in its resting state. Structure 13 (2005) 703-712
    • (2005) Structure , vol.13 , pp. 703-712
    • Gottschalk, K.E.1
  • 106
    • 2942587504 scopus 로고    scopus 로고
    • A computational model of transmembrane integrin clustering
    • Gottschalk K.E., and Kessler H. A computational model of transmembrane integrin clustering. Structure 12 (2004) 1109-1116
    • (2004) Structure , vol.12 , pp. 1109-1116
    • Gottschalk, K.E.1    Kessler, H.2
  • 107
    • 1642573163 scopus 로고    scopus 로고
    • Evidence for hetero-association of transmembrane helices of integrins
    • Gottschalk K.E., and Kessler H. Evidence for hetero-association of transmembrane helices of integrins. FEBS Lett 557 (2004) 253-258
    • (2004) FEBS Lett , vol.557 , pp. 253-258
    • Gottschalk, K.E.1    Kessler, H.2
  • 108
    • 14844346910 scopus 로고    scopus 로고
    • Disrupting integrin transmembrane domain heterodimerization increases ligand binding affinity, not valency or clustering
    • Luo B.H., Carman C.V., Takagi J., and Springer T.A. Disrupting integrin transmembrane domain heterodimerization increases ligand binding affinity, not valency or clustering. Proc Natl Acad Sci USA 102 (2005) 3679-3684
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3679-3684
    • Luo, B.H.1    Carman, C.V.2    Takagi, J.3    Springer, T.A.4
  • 109
    • 34147130190 scopus 로고    scopus 로고
    • Computational design of peptides that target transmembrane helices
    • An intriguing new pharmacological approach to structural and functional analysis of protein transmembrane domains.
    • Yin H., Slusky J.S., Berger B.W., Walters R.S., Vilaire G., Litvinov R.I., Lear J.D., Caputo G.A., Bennett J.S., and DeGrado W.F. Computational design of peptides that target transmembrane helices. Science 315 (2007) 1817-1822. An intriguing new pharmacological approach to structural and functional analysis of protein transmembrane domains.
    • (2007) Science , vol.315 , pp. 1817-1822
    • Yin, H.1    Slusky, J.S.2    Berger, B.W.3    Walters, R.S.4    Vilaire, G.5    Litvinov, R.I.6    Lear, J.D.7    Caputo, G.A.8    Bennett, J.S.9    DeGrado, W.F.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.