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Volumn 15, Issue 5, 2003, Pages 547-556

Integrin avidity regulation: Are changes in affinity and conformation underemphasized?

Author keywords

[No Author keywords available]

Indexed keywords

INTEGRIN;

EID: 0141756175     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2003.08.003     Document Type: Review
Times cited : (443)

References (86)
  • 1
    • 0031952651 scopus 로고    scopus 로고
    • Are changes in integrin affinity and conformation overemphasized?
    • Bazzoni G., Hemler M.E. Are changes in integrin affinity and conformation overemphasized? Trends Biochem Sci. 23:1998;30-34.
    • (1998) Trends Biochem Sci , vol.23 , pp. 30-34
    • Bazzoni, G.1    Hemler, M.E.2
  • 2
    • 0024443411 scopus 로고
    • T cell receptor cross-linking transiently stimulates adhesiveness through LFA-1
    • Dustin M.L., Springer T.A. T cell receptor cross-linking transiently stimulates adhesiveness through LFA-1. Nature. 341:1989;619-624.
    • (1989) Nature , vol.341 , pp. 619-624
    • Dustin, M.L.1    Springer, T.A.2
  • 3
    • 0003846050 scopus 로고
    • Hagerstown, MD: Harper and Row, Publishers
    • Eisen HN: Immunology, edn 2. Hagerstown, MD: Harper and Row, Publishers; 1980.
    • (1980) Immunology, Edn 2
    • Eisen, H.N.1
  • 5
    • 0026598574 scopus 로고
    • Intercellular communication and cell-cell adhesion
    • Singer S.J. Intercellular communication and cell-cell adhesion. Science. 255:1992;1671-1677.
    • (1992) Science , vol.255 , pp. 1671-1677
    • Singer, S.J.1
  • 6
    • 0036697001 scopus 로고    scopus 로고
    • Integrin activation and structural rearrangement
    • Takagi J., Springer T.A. Integrin activation and structural rearrangement. Immunol Rev. 186:2002;141-163.
    • (2002) Immunol Rev , vol.186 , pp. 141-163
    • Takagi, J.1    Springer, T.A.2
  • 7
    • 0024293497 scopus 로고
    • Electron microscopy and structural model of human fibronectin receptor
    • Nermut M.V., Green N.M., Eason P., Yamada S.S., Yamada K.M. Electron microscopy and structural model of human fibronectin receptor. EMBO J. 7:1988;4093-4099.
    • (1988) EMBO J , vol.7 , pp. 4093-4099
    • Nermut, M.V.1    Green, N.M.2    Eason, P.3    Yamada, S.S.4    Yamada, K.M.5
  • 8
    • 0035850669 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin αVβ3
    • This is the watershed description of the structure of most of the integrin extracellular domain, which displayed an unexpected V-shaped topology arising from a severe bend in the stalks termed the 'genu'.
    • Xiong J.-P., Stehle T., Diefenbach B., Zhang R., Dunker R., Scott D.L., Joachimiak A., Goodman S.L., Arnaout M.A. Crystal structure of the extracellular segment of integrin αVβ3. Science. 294:2001;339-345 This is the watershed description of the structure of most of the integrin extracellular domain, which displayed an unexpected V-shaped topology arising from a severe bend in the stalks termed the 'genu'.
    • (2001) Science , vol.294 , pp. 339-345
    • Xiong, J.-P.1    Stehle, T.2    Diefenbach, B.3    Zhang, R.4    Dunker, R.5    Scott, D.L.6    Joachimiak, A.7    Goodman, S.L.8    Arnaout, M.A.9
  • 9
    • 0035805633 scopus 로고    scopus 로고
    • Association of the membrane-proximal regions of the α and β subunit cytoplasmic domains constrains an integrin in the inactive state
    • Lu C., Takagi J., Springer T.A. Association of the membrane-proximal regions of the α and β subunit cytoplasmic domains constrains an integrin in the inactive state. J Biol Chem. 276:2001;14642-14648.
    • (2001) J Biol Chem , vol.276 , pp. 14642-14648
    • Lu, C.1    Takagi, J.2    Springer, T.A.3
  • 10
    • 0036220127 scopus 로고    scopus 로고
    • Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation
    • •• ]. Localization of activation epitopes to sterically inaccessible surfaces in the bent integrin suggested that this conformation represents the low-affinity state. A switchblade-like rearrangement was suggested to occur during activation that would make the epitopes accessible for antibody recognition.
    • ••]. Localization of activation epitopes to sterically inaccessible surfaces in the bent integrin suggested that this conformation represents the low-affinity state. A switchblade-like rearrangement was suggested to occur during activation that would make the epitopes accessible for antibody recognition.
    • (2002) Nat Struct Biol , vol.9 , pp. 282-287
    • Beglova, N.1    Blacklow, S.C.2    Takagi, J.3    Springer, T.A.4
  • 11
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling
    • 2+ induced a switchblade-like extension of the integrin, with a mixture of closed and open headpiece orientations. Cyclic RGD exclusively produced the extended conformer with the open headpiece. Stabilization of the bent conformation on the cell surface by an engineered disulfide bond prevented activation.
    • 2+ induced a switchblade-like extension of the integrin, with a mixture of closed and open headpiece orientations. Cyclic RGD exclusively produced the extended conformer with the open headpiece. Stabilization of the bent conformation on the cell surface by an engineered disulfide bond prevented activation.
    • (2002) Cell , vol.110 , pp. 599-611
    • Takagi, J.1    Petre, B.M.2    Walz, T.3    Springer, T.A.4
  • 12
    • 0035041854 scopus 로고    scopus 로고
    • C-terminal opening mimics 'inside-out' activation of integrin α5β1
    • Rotary-shadowed electron microscopy, together with surface plasmon resonance and solid-phase equilibrium ligand-binding studies, were performed on soluble extracellular domain α5β1 heterodimer with an engineered protease-cleavable clasp replacing the transmembrane and cytoplasmic domains. Release of the clasp induced a substantial separation of the stalks that was coupled to a significant increase in affinity for ligand.
    • Takagi J., Erickson H.P., Springer T.A. C-terminal opening mimics 'inside-out' activation of integrin α5β1. Nat Struct Biol. 8:2001;412-416 Rotary-shadowed electron microscopy, together with surface plasmon resonance and solid-phase equilibrium ligand-binding studies, were performed on soluble extracellular domain α5β1 heterodimer with an engineered protease-cleavable clasp replacing the transmembrane and cytoplasmic domains. Release of the clasp induced a substantial separation of the stalks that was coupled to a significant increase in affinity for ligand.
    • (2001) Nat Struct Biol , vol.8 , pp. 412-416
    • Takagi, J.1    Erickson, H.P.2    Springer, T.A.3
  • 14
    • 0037418254 scopus 로고    scopus 로고
    • Stabilizing the open conformation of the integrin headpiece with a glycan wedge increases affinity for ligand
    • Ectopic N-linked glycosylation sites were mutationally introduced into a loop at the bottom of the β1 and β3 I-like domains to serve as 'wedges', enforcing the open headpiece conformation. In the context of α5β1 and αIIβ3, these mutations induced constitutive high affinity for ligand. A model for I-like domain activation, driven by downward translation of the carboxy-terminal helix and swing-out of the hybrid domain, was suggested.
    • Luo B.-H., Springer T.A., Takagi J. Stabilizing the open conformation of the integrin headpiece with a glycan wedge increases affinity for ligand. Proc Natl Acad Sci USA. 100:2003;2403-2408 Ectopic N-linked glycosylation sites were mutationally introduced into a loop at the bottom of the β1 and β3 I-like domains to serve as 'wedges', enforcing the open headpiece conformation. In the context of α5β1 and αIIβ3, these mutations induced constitutive high affinity for ligand. A model for I-like domain activation, driven by downward translation of the carboxy-terminal helix and swing-out of the hybrid domain, was suggested.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 2403-2408
    • Luo, B.-H.1    Springer, T.A.2    Takagi, J.3
  • 15
  • 18
    • 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., 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
  • 19
  • 20
    • 0035956969 scopus 로고    scopus 로고
    • An isolated, surface-expressed I domain of the integrin αLβ2 is sufficient for strong adhesive function when locked in the open conformation with a disulfide
    • Lu C., Shimaoka M., Ferzly M., Oxvig C., Takagi J., Springer T.A. An isolated, surface-expressed I domain of the integrin αLβ2 is sufficient for strong adhesive function when locked in the open conformation with a disulfide. Proc Natl Acad Sci USA. 98:2001;2387-2392.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2387-2392
    • Lu, C.1    Shimaoka, M.2    Ferzly, M.3    Oxvig, C.4    Takagi, J.5    Springer, T.A.6
  • 21
    • 0035956887 scopus 로고    scopus 로고
    • Locking in alternate conformations of the integrin αLβ2 I domain with disulfide bonds reveals functional relationships among integrin domains
    • Lu C., Shimaoka M., Zang Q., Takagi J., Springer T.A. Locking in alternate conformations of the integrin αLβ2 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
  • 22
    • 0033900165 scopus 로고    scopus 로고
    • Computational design of an integrin I domain stabilized in the open, high affinity conformation
    • Shimaoka M., Shifman J.M., Jing H., Takagi J., Mayo S.L., Springer T.A. Computational design of an integrin I domain stabilized in the open, high affinity conformation. Nat Struct Biol. 7:2000;674-678.
    • (2000) Nat Struct Biol , vol.7 , pp. 674-678
    • Shimaoka, M.1    Shifman, J.M.2    Jing, H.3    Takagi, J.4    Mayo, S.L.5    Springer, T.A.6
  • 23
    • 0035932996 scopus 로고    scopus 로고
    • Reversibly locking a protein fold in an active conformation with a disulfide bond: Integrin αL I domains with high affinity and antagonist activity in vivo
    • Disulfide bonds that bracket the carboxy-terminal β6-α7 loop and stabilize the open conformation of the αL I domain result in a 10,000-fold increase in affinity for ICAM-1, as determined by surface plasmon resonance.
    • Shimaoka M., Lu C., Palframan R., von Andrian U.H., Takagi J., Springer T.A. Reversibly locking a protein fold in an active conformation with a disulfide bond: integrin αL I domains with high affinity and antagonist activity in vivo. Proc Natl Acad Sci USA. 98:2001;6009-6014 Disulfide bonds that bracket the carboxy-terminal β6-α7 loop and stabilize the open conformation of the αL I domain result in a 10,000-fold increase in affinity for ICAM-1, as determined by surface plasmon resonance.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6009-6014
    • Shimaoka, M.1    Lu, C.2    Palframan, R.3    Von Andrian, U.H.4    Takagi, J.5    Springer, T.A.6
  • 24
    • 0037168524 scopus 로고    scopus 로고
    • Stabilizing the integrin αM inserted domain in alternative conformations with a range of engineered disulfide bonds
    • Shimaoka M., Lu C., Salas A., Xiao T., Takagi J., Springer T.A. Stabilizing the integrin αM inserted domain in alternative conformations with a range of engineered disulfide bonds. Proc Natl Acad Sci USA. 99:2002;16737-16741.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16737-16741
    • Shimaoka, M.1    Lu, C.2    Salas, A.3    Xiao, T.4    Takagi, J.5    Springer, T.A.6
  • 25
    • 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., 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
  • 27
    • 0033515012 scopus 로고    scopus 로고
    • Conformational changes in tertiary structure near the ligand binding site of an integrin I domain
    • Oxvig C., Lu C., Springer T.A. Conformational changes in tertiary structure near the ligand binding site of an integrin I domain. Proc Natl Acad Sci USA. 96:1999;2215-2220.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 2215-2220
    • Oxvig, C.1    Lu, C.2    Springer, T.A.3
  • 28
    • 0037155910 scopus 로고    scopus 로고
    • Activation induced conformational changes in the I domain region of LFA-1
    • Ma Q., Shimaoka M., Lu C., Jing H., Carman C.V., Springer T.A. Activation induced conformational changes in the I domain region of LFA-1. J Biol Chem. 277:2002;10638-10641.
    • (2002) J Biol Chem , vol.277 , pp. 10638-10641
    • Ma, Q.1    Shimaoka, M.2    Lu, C.3    Jing, H.4    Carman, C.V.5    Springer, T.A.6
  • 29
    • 0032922549 scopus 로고    scopus 로고
    • A novel leukocyte adhesion deficiency caused by expressed but nonfunctional β2 integrins Mac-1 and LFA-1
    • Hogg N., Stewart M.P., Scarth S.L., Newton R., Shaw J.M., Law S.K.A., Klein N. A novel leukocyte adhesion deficiency caused by expressed but nonfunctional β2 integrins Mac-1 and LFA-1. J Clin Invest. 103:1999;97-106.
    • (1999) J Clin Invest , vol.103 , pp. 97-106
    • Hogg, N.1    Stewart, M.P.2    Scarth, S.L.3    Newton, R.4    Shaw, J.M.5    Law, S.K.A.6    Klein, N.7
  • 30
    • 0141746138 scopus 로고    scopus 로고
    • Small molecule integrin antagonists that bind to the β2 subunit I-like domain and activate signals in one direction and block them in another
    • in press
    • Shimaoka M, Salas A, Yang W, Weitz-Schmidt G, Springer TA: Small molecule integrin antagonists that bind to the β2 subunit I-like domain and activate signals in one direction and block them in another. Immunity 2003, in press.
    • (2003) Immunity
    • Shimaoka, M.1    Salas, A.2    Yang, W.3    Weitz-Schmidt, G.4    Springer, T.A.5
  • 34
    • 0037389585 scopus 로고    scopus 로고
    • An unraveling tale of how integrins are activated from within
    • Travis M.A., Humphries J.D., Humphries M.J. An unraveling tale of how integrins are activated from within. Trends Pharmacol Sci. 24:2003;192-197.
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 192-197
    • Travis, M.A.1    Humphries, J.D.2    Humphries, M.J.3
  • 35
    • 0037195164 scopus 로고    scopus 로고
    • Three-dimensional model of the human platelet integrin αIIbβ3 based on electron cryomicroscopy and X-ray crystallography
    • Adair B.D., Yeager M. Three-dimensional model of the human platelet integrin αIIbβ3 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
  • 36
    • 0037031551 scopus 로고    scopus 로고
    • 3 'inside-out' activation as regulated by its cytoplasmic face
    • Nuclear magnetic resonance structural analysis demonstrated the formation of a direct association between the αIIb and β3 cytoplasmic tails that was disrupted by the talin head domain and activating mutations.
    • 3 'inside-out' activation as regulated by its cytoplasmic face. Cell. 110:2002;587-597 Nuclear magnetic resonance structural analysis demonstrated the formation of a direct association between the αIIb and β3 cytoplasmic tails that was disrupted by the talin head domain and activating mutations.
    • (2002) Cell , vol.110 , pp. 587-597
    • Vinogradova, O.1    Velyvis, A.2    Velyviene, A.3    Hu, B.4    Haas, T.A.5    Plow, E.F.6    Qin, J.7
  • 37
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • in press
    • Kim M, Carman CV, Springer TA: Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science 2003, in press.
    • (2003) Science
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 38
    • 0037593914 scopus 로고    scopus 로고
    • High affinity ligand binding by integrins does not involve head separation
    • Luo B.-H., Springer T.A., Takagi J. High affinity ligand binding by integrins does not involve head separation. J Biol Chem. 278:2003;17185-17189.
    • (2003) J Biol Chem , vol.278 , pp. 17185-17189
    • Luo, B.-H.1    Springer, T.A.2    Takagi, J.3
  • 39
    • 0030917144 scopus 로고    scopus 로고
    • Flow cytometric measurement of kinetic and equilibrium binding parameters of arginine-glycine-aspartic acid ligands in binding to glycoprotein IIb/IIIa on platelets
    • Bednar B., Cunningham M.E., McQueney P.A., Egbertson M.S., Askew B.C., Bednar R.A., Hartman G.D., Gould R.J. Flow cytometric measurement of kinetic and equilibrium binding parameters of arginine-glycine-aspartic acid ligands in binding to glycoprotein IIb/IIIa on platelets. Cytometry. 28:1997;58-65.
    • (1997) Cytometry , vol.28 , pp. 58-65
    • Bednar, B.1    Cunningham, M.E.2    McQueney, P.A.3    Egbertson, M.S.4    Askew, B.C.5    Bednar, R.A.6    Hartman, G.D.7    Gould, R.J.8
  • 40
    • 0027467279 scopus 로고
    • Two-step binding mechanism of fibrinogen to alpha IIb beta 3 integrin reconstituted into planar lipid bilayers
    • Muller B., Zerwes H.G., Tangemann K., Peter J., Engel J. Two-step binding mechanism of fibrinogen to alpha IIb beta 3 integrin reconstituted into planar lipid bilayers. J Biol Chem. 268:1993;6800-6808.
    • (1993) J Biol Chem , vol.268 , pp. 6800-6808
    • Muller, B.1    Zerwes, H.G.2    Tangemann, K.3    Peter, J.4    Engel, J.5
  • 41
    • 0028869590 scopus 로고
    • Determination of kinetic constants for the interaction between the platelet glycoprotein IIb-IIIa and fibrinogen by means of surface plasmon resonance
    • Huber W., Hurst J., Schlatter D., Barner R., Hübscher J., Kouns W.C., Steiner B. Determination of kinetic constants for the interaction between the platelet glycoprotein IIb-IIIa and fibrinogen by means of surface plasmon resonance. Eur J Biochem. 227:1995;647-656.
    • (1995) Eur J Biochem , vol.227 , pp. 647-656
    • Huber, W.1    Hurst, J.2    Schlatter, D.3    Barner, R.4    Hübscher, J.5    Kouns, W.C.6    Steiner, B.7
  • 42
    • 0034507687 scopus 로고    scopus 로고
    • Chemokines trigger immediate β2 integrin affinity and mobility changes: Differential regulation and roles in lymphocyte arrest under flow
    • Constantin G., Majeed M., Giagulli C., Piccib L., Kim J.Y., Butcher E.C., Laudanna C. Chemokines trigger immediate β2 integrin affinity and mobility changes: differential regulation and roles in lymphocyte arrest under flow. Immunity. 13:2000;759-769.
    • (2000) Immunity , vol.13 , pp. 759-769
    • Constantin, G.1    Majeed, M.2    Giagulli, C.3    Piccib, L.4    Kim, J.Y.5    Butcher, E.C.6    Laudanna, C.7
  • 43
    • 0035927140 scopus 로고    scopus 로고
    • Chemoattractants induce rapid and transient upregulation of monocyte alpha4 integrin affinity for vascular adhesion molecule 1 which mediates arrest: An early step in the process of emigration
    • Chan J.R., Hyduk S.J., Cybulsky M.I. Chemoattractants induce rapid and transient upregulation of monocyte alpha4 integrin affinity for vascular adhesion molecule 1 which mediates arrest: an early step in the process of emigration. J Exp Med. 193:2001;1149-1158.
    • (2001) J Exp Med , vol.193 , pp. 1149-1158
    • Chan, J.R.1    Hyduk, S.J.2    Cybulsky, M.I.3
  • 44
    • 0037299727 scopus 로고    scopus 로고
    • Detecting rapid and transient upregulation of leukocyte integrin affinity induced by chemokines and chemoattractants
    • Chan J.R., Hyduk S.J., Cybulsky M.I. Detecting rapid and transient upregulation of leukocyte integrin affinity induced by chemokines and chemoattractants. J Immunol Methods. 273:2003;43-52.
    • (2003) J Immunol Methods , vol.273 , pp. 43-52
    • Chan, J.R.1    Hyduk, S.J.2    Cybulsky, M.I.3
  • 46
    • 0033824065 scopus 로고    scopus 로고
    • Avidity regulation of integrins: The driving force in leukocyte adhesion
    • van Kooyk Y., Figdor C.G. Avidity regulation of integrins: the driving force in leukocyte adhesion. Curr Opin Cell Biol. 12:2000;542-547.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 542-547
    • Van Kooyk, Y.1    Figdor, C.G.2
  • 48
    • 0032528432 scopus 로고    scopus 로고
    • Molecular regulation of the interaction between leukocyte function-associated antigen-1 and soluble ICAM-1 by divalent metal cations
    • Labadia M.E., Jeanfavre D.D., Caviness G.O., Morelock M.M. Molecular regulation of the interaction between leukocyte function-associated antigen-1 and soluble ICAM-1 by divalent metal cations. J Immunol. 161:1998;836-842.
    • (1998) J Immunol , vol.161 , pp. 836-842
    • Labadia, M.E.1    Jeanfavre, D.D.2    Caviness, G.O.3    Morelock, M.M.4
  • 49
    • 0027364840 scopus 로고
    • Direct evidence for two affinity states for lymphocyte function-associated antigen 1 on activated T cells
    • Lollo B.A., Chan K.W.H., Hanson E.M., Moy V.T., Brian A.A. Direct evidence for two affinity states for lymphocyte function-associated antigen 1 on activated T cells. J Biol Chem. 268:1993;21693-21700.
    • (1993) J Biol Chem , vol.268 , pp. 21693-21700
    • Lollo, B.A.1    Chan, K.W.H.2    Hanson, E.M.3    Moy, V.T.4    Brian, A.A.5
  • 51
    • 0028978448 scopus 로고
    • 2+- and calcineurin-dependent recycling of an integrin to the front of migrating neutrophils
    • 2+- and calcineurin-dependent recycling of an integrin to the front of migrating neutrophils. Nature. 377:1995;75-79.
    • (1995) Nature , vol.377 , pp. 75-79
    • Lawson, M.A.1    Maxfield, F.R.2
  • 52
    • 0038647351 scopus 로고    scopus 로고
    • The critical cytoplasmic regions of the αL/β2 integrin in Rap1-induced adhesion and migration
    • Tohyama Y., Katagiri K., Pardi R., Lu C., Springer T.A., Kinashi T. The critical cytoplasmic regions of the αL/β2 integrin in Rap1-induced adhesion and migration. Mol Biol Cell. 14:2003;2570-2582.
    • (2003) Mol Biol Cell , vol.14 , pp. 2570-2582
    • Tohyama, Y.1    Katagiri, K.2    Pardi, R.3    Lu, C.4    Springer, T.A.5    Kinashi, T.6
  • 53
    • 0042490495 scopus 로고    scopus 로고
    • RAPL, a novel Rap1-binding molecule, mediates Rap1-induced adhesion through spatial regulation of LFA-1
    • in press
    • Katagiri K, Maeda A, Shimonaka M, Kinashi T: RAPL, a novel Rap1-binding molecule, mediates Rap1-induced adhesion through spatial regulation of LFA-1. Nat Immunol 2003, in press.
    • (2003) Nat Immunol
    • Katagiri, K.1    Maeda, A.2    Shimonaka, M.3    Kinashi, T.4
  • 54
    • 0038561221 scopus 로고    scopus 로고
    • Rap1 translates chemokine signals to integrin activation, cell polarization, and motility across vascular endothelium under flow
    • Chemokines activated both Rap1- and LFA-1-dependent adhesiveness in lymphocytes. Overexpression of the Rap1 GTPase-activating protein Spa1 abrogated the effects of chemokine. Expression of constitutively active Rap1 (Rap1V12) promoted transmigration and polarization of CD44 and CXCR4 to the uropod and leading edge, respectively.
    • Shimonaka M., Katagiri K., Kakayama T., Fujita N., Tsuruo T., Yoshie O., Kinashi T. Rap1 translates chemokine signals to integrin activation, cell polarization, and motility across vascular endothelium under flow. J Cell Biol. 161:2003;417-427 Chemokines activated both Rap1- and LFA-1-dependent adhesiveness in lymphocytes. Overexpression of the Rap1 GTPase-activating protein Spa1 abrogated the effects of chemokine. Expression of constitutively active Rap1 (Rap1V12) promoted transmigration and polarization of CD44 and CXCR4 to the uropod and leading edge, respectively.
    • (2003) J Cell Biol , vol.161 , pp. 417-427
    • Shimonaka, M.1    Katagiri, K.2    Kakayama, T.3    Fujita, N.4    Tsuruo, T.5    Yoshie, O.6    Kinashi, T.7
  • 55
    • 0036500126 scopus 로고    scopus 로고
    • The involvement of lipid rafts in the regulation of integrins function
    • Leitinger B., Hogg N. The involvement of lipid rafts in the regulation of integrins function. J Cell Sci. 115:2002;963-972.
    • (2002) J Cell Sci , vol.115 , pp. 963-972
    • Leitinger, B.1    Hogg, N.2
  • 57
    • 0037131185 scopus 로고    scopus 로고
    • 4 integrin avidity but not leukocyte functional-associated antigen-1 avidity to endothelial ligands under shear flow requires cholesterol membrane rafts
    • 4 integrin avidity but not leukocyte functional-associated antigen-1 avidity to endothelial ligands under shear flow requires cholesterol membrane rafts. J Biol Chem. 277:2002;40027-40035.
    • (2002) J Biol Chem , vol.277 , pp. 40027-40035
    • Shamri, R.1    Grabovinsky, V.2    Feigelson, S.W.3    Dwir, O.4    Van Kooyk, Y.5    Alon, R.6
  • 58
    • 0033601228 scopus 로고    scopus 로고
    • Integrin leukocyte function-associated antigen-1-mediated cell binding can be activated by clustering of membrane rafts
    • Krauss K., Altevogt P. Integrin leukocyte function-associated antigen-1-mediated cell binding can be activated by clustering of membrane rafts. J Biol Chem. 274:1999;36921-36927.
    • (1999) J Biol Chem , vol.274 , pp. 36921-36927
    • Krauss, K.1    Altevogt, P.2
  • 59
    • 0035940359 scopus 로고    scopus 로고
    • Oligomerization of the integrin αIIbβ3: Roles of the transmembrane and cytoplasmic domains
    • Li R., Babu C.R., Lear J.D., Wand A.J., Bennett J.S., Degrado W.F. Oligomerization of the integrin αIIbβ3: roles of the transmembrane and cytoplasmic domains. Proc Natl Acad Sci USA. 98:2001;12462-12467.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12462-12467
    • Li, R.1    Babu, C.R.2    Lear, J.D.3    Wand, A.J.4    Bennett, J.S.5    Degrado, W.F.6
  • 61
    • 0029913643 scopus 로고    scopus 로고
    • Adhesion-activating phorbol ester increases the mobility of leukocyte integrin LFA-1 in cultured lymphocytes
    • Kucik D.F., Dustin M.L., Miller J.M., Brown E.J. Adhesion-activating phorbol ester increases the mobility of leukocyte integrin LFA-1 in cultured lymphocytes. J Clin Invest. 97:1996;2139-2144.
    • (1996) J Clin Invest , vol.97 , pp. 2139-2144
    • Kucik, D.F.1    Dustin, M.L.2    Miller, J.M.3    Brown, E.J.4
  • 62
    • 0037674763 scopus 로고    scopus 로고
    • Detection of integrin αIIbβ3 clustering in living cells
    • αIIb cytoplasmic chimeras with β-galactosidase half-domains, luciferase and green fluorescent protein were used to measure αIIbβ3 microclustering by β-galactosidase complementation or BRET. Multivalent ligand (fibrinogen) produced microclustering that was facilitated by disruption of the actin cytoskeleton.
    • Buensuceso C., De Virgilio M., Shattil S.J. Detection of integrin αIIbβ3 clustering in living cells. J Biol Chem. 278:2003;15217-15224 αIIb cytoplasmic chimeras with β-galactosidase half-domains, luciferase and green fluorescent protein were used to measure αIIbβ3 microclustering by β-galactosidase complementation or BRET. Multivalent ligand (fibrinogen) produced microclustering that was facilitated by disruption of the actin cytoskeleton.
    • (2003) J Biol Chem , vol.278 , pp. 15217-15224
    • Buensuceso, C.1    De Virgilio, M.2    Shattil, S.J.3
  • 63
    • 0035878668 scopus 로고    scopus 로고
    • Green fluorescent protein (GFP) tagged to the cytoplasmic tail of αIIb or β3 allows the expression of a fully functional integrin αIIβ3: Effect of β3GFP on αIIbβ3 ligand binding
    • Plancon S., Morel-Kopp M.C., Schaffner-Reckinger E., Chen P., Kieffer N. Green fluorescent protein (GFP) tagged to the cytoplasmic tail of αIIb or β3 allows the expression of a fully functional integrin αIIβ3: effect of β3GFP on αIIbβ3 ligand binding. Biochem J. 357:2001;529-536.
    • (2001) Biochem J , vol.357 , pp. 529-536
    • Plancon, S.1    Morel-Kopp, M.C.2    Schaffner-Reckinger, E.3    Chen, P.4    Kieffer, N.5
  • 64
    • 0035954424 scopus 로고    scopus 로고
    • Differential dynamics of α5 integrin, paxillin, and α-actinin during formation and disassembly of adhesions in migrating cells
    • Laukaitis C.M., Webb D.J., Donais K., Horwitz A.F. Differential dynamics of α5 integrin, paxillin, and α-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
  • 65
    • 0037077282 scopus 로고    scopus 로고
    • The phosphotyrosine binding (PTB)-like domain of talin activates integrins
    • The phosphotyrosine binding domain of talin was shown to directly bind to the β3 cytoplasmic tail NPXY motif and to induce binding of the ligand-mimetic antibody PAC1 to cell-surface αIIbβ3.
    • Calderwood D.A., Yan B., de Pereda J.M., Garcia-Alvarez B., Fujioka Y., Liddington R.C., Ginsberg M.H. The phosphotyrosine binding (PTB)-like domain of talin activates integrins. J Biol Chem. 277:2002;21749-21758 The phosphotyrosine binding domain of talin was shown to directly bind to the β3 cytoplasmic tail NPXY motif and to induce binding of the ligand-mimetic antibody PAC1 to cell-surface αIIbβ3.
    • (2002) J Biol Chem , vol.277 , pp. 21749-21758
    • Calderwood, D.A.1    Yan, B.2    De Pereda, J.M.3    Garcia-Alvarez, B.4    Fujioka, Y.5    Liddington, R.C.6    Ginsberg, M.H.7
  • 66
    • 0033213922 scopus 로고    scopus 로고
    • The talin head domain binds to integrin β subunit cytoplasmic tails and regulates integrin activation
    • Calderwood D.A., Zent R., Grant R., Rees D.J., Hynes R.O., Ginsberg M.H. The talin head domain binds to integrin β subunit cytoplasmic tails and regulates integrin activation. J Biol Chem. 274:1999;28071-28074.
    • (1999) J Biol Chem , vol.274 , pp. 28071-28074
    • Calderwood, D.A.1    Zent, R.2    Grant, R.3    Rees, D.J.4    Hynes, R.O.5    Ginsberg, M.H.6
  • 67
    • 0037238844 scopus 로고    scopus 로고
    • Structural determinants of integrin recognition by talin
    • X-ray crystal structure and nuclear magnetic resonance analysis demonstrate the binding of the talin phosphotyrosine binding domain to the β3 cytoplasmic tail via an NPXY motif and membrane-proximal residues that are near the end of the major helical segment observed in the α-β complex [35]. The authors suggest a two-step model for talin binding and activation of integrins.
    • Garcia-Alvarez B., de Pereda J.M., Calderwood D.A., Ulmer T.S., Critchley D., Campbell I.D., Ginsberg M.H., Liddington R.C. Structural determinants of integrin recognition by talin. Mol Cell. 11:2003;49-58 X-ray crystal structure and nuclear magnetic resonance analysis demonstrate the binding of the talin phosphotyrosine binding domain to the β3 cytoplasmic tail via an NPXY motif and membrane-proximal residues that are near the end of the major helical segment observed in the α-β complex [35]. The authors suggest a two-step model for talin binding and activation of integrins.
    • (2003) Mol Cell , vol.11 , pp. 49-58
    • Garcia-Alvarez, B.1    De Pereda, J.M.2    Calderwood, D.A.3    Ulmer, T.S.4    Critchley, D.5    Campbell, I.D.6    Ginsberg, M.H.7    Liddington, R.C.8
  • 68
    • 0035958967 scopus 로고    scopus 로고
    • Calpain cleavage promotes talin binding to the β3 integrin cytoplasmic domain
    • Yan B., Calderwood D.A., Yaspan B., Ginsberg M.H. Calpain cleavage promotes talin binding to the β3 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
  • 72
    • 0034004457 scopus 로고    scopus 로고
    • Rap1 is a potent activation signal for leukocyte function-associated antigen 1 distinct from protein kinase C and phosphatidylinositol-3-OH kinase
    • Katagiri K., Hattori M., Minato N., Irie S., Takatsu K., Kinashi T. Rap1 is a potent activation signal for leukocyte function-associated antigen 1 distinct from protein kinase C and phosphatidylinositol-3-OH kinase. Mol Cell Biol. 20:2000;1956-1969.
    • (2000) Mol Cell Biol , vol.20 , pp. 1956-1969
    • Katagiri, K.1    Hattori, M.2    Minato, N.3    Irie, S.4    Takatsu, K.5    Kinashi, T.6
  • 73
    • 0036146452 scopus 로고    scopus 로고
    • Rap1 functions as a key regulator of T-cell and antigen-presenting cell interactions and modulates T-cell responses
    • Katagiri K., Hattori M., Minato N., Kinashi T. Rap1 functions as a key regulator of T-cell and antigen-presenting cell interactions and modulates T-cell responses. Mol Cell Biol. 22:2002;1001-1015.
    • (2002) Mol Cell Biol , vol.22 , pp. 1001-1015
    • Katagiri, K.1    Hattori, M.2    Minato, N.3    Kinashi, T.4
  • 74
    • 0037067748 scopus 로고    scopus 로고
    • Relationships between Rap1b, affinity modulation of integrin αIIbβ3, and the actin cytoskeleton
    • Bertoni A., Tadokoro S., Eto K., Pampori N., Parise L.V., White G.C., Shattil S.J. Relationships between Rap1b, affinity modulation of integrin αIIbβ3, and the actin cytoskeleton. J Biol Chem. 277:2002; 25715-25721.
    • (2002) J Biol Chem , vol.277 , pp. 25715-25721
    • Bertoni, A.1    Tadokoro, S.2    Eto, K.3    Pampori, N.4    Parise, L.V.5    White, G.C.6    Shattil, S.J.7
  • 75
    • 0037119416 scopus 로고    scopus 로고
    • The small GTPase Rap1 is required for Mn(2+)- and antibody-induced LFA-1- and VLA-4-mediated cell adhesion
    • de Bruyn K.M., Rangarajan S., Reedquist K.A., Figdor C.G., Bos J.L. The small GTPase Rap1 is required for Mn(2+)- and antibody-induced LFA-1- and VLA-4-mediated cell adhesion. J Biol Chem. 277:2002;29468-29476.
    • (2002) J Biol Chem , vol.277 , pp. 29468-29476
    • De Bruyn, K.M.1    Rangarajan, S.2    Reedquist, K.A.3    Figdor, C.G.4    Bos, J.L.5
  • 77
    • 0036009116 scopus 로고    scopus 로고
    • Rap1A positively regulates T cells via integrin activation rather than inhibiting lymphocyte signaling
    • Primary T cells from transgenic mice expressing constitutively active Rap1A exhibited potentiated T-cell receptor responses and constitutively adhesive LFA-1, VLA-4 and VLA-5.
    • Sebzda E., Bracke M., Tugal T., Hogg N., Cantrell D.A. Rap1A positively regulates T cells via integrin activation rather than inhibiting lymphocyte signaling. Nat Immunol. 3:2002;251-258 Primary T cells from transgenic mice expressing constitutively active Rap1A exhibited potentiated T-cell receptor responses and constitutively adhesive LFA-1, VLA-4 and VLA-5.
    • (2002) Nat Immunol , vol.3 , pp. 251-258
    • Sebzda, E.1    Bracke, M.2    Tugal, T.3    Hogg, N.4    Cantrell, D.A.5
  • 78
    • 0034745356 scopus 로고    scopus 로고
    • Rac recruits high affinity integrin αVβ3 to lamellipodia in endothelial cell migration
    • Kiosses W.B., Shattil S.J., Pampori N., Schwartz M.A. Rac recruits high affinity integrin αVβ3 to lamellipodia in endothelial cell migration. Nat Cell Biol. 3:2001;316-320.
    • (2001) Nat Cell Biol , vol.3 , pp. 316-320
    • Kiosses, W.B.1    Shattil, S.J.2    Pampori, N.3    Schwartz, M.A.4
  • 79
    • 0041384357 scopus 로고    scopus 로고
    • LFA-1-induced T cell migration on ICAM-1 involves regulation of MLCK-mediated attachment and ROCK-dependent detachment
    • Epub.
    • Smith A, Bracke M, Leitinger B, Porter JC, Hogg N: LFA-1-induced T cell migration on ICAM-1 involves regulation of MLCK-mediated attachment and ROCK-dependent detachment. J Cell Sci 2003, Epub.
    • (2003) J Cell Sci
    • Smith, A.1    Bracke, M.2    Leitinger, B.3    Porter, J.C.4    Hogg, N.5
  • 80
    • 0035833247 scopus 로고    scopus 로고
    • RhoA is required for monocyte tail retraction during transendothelial migration
    • Inhibition of RhoA or its kinase effector p160ROCK specifically inhibited monocyte tail retraction and caused accumulation of β2 integrins in the uropod. Whereas adhesion to ICAM-1 and VCAM-1 was significantly enhanced by p160ROCK inhibition, it was reduced by constitutively active p160ROCK.
    • Worthylake R.A., Lemoine S., Watson J.M., Burridge K. RhoA is required for monocyte tail retraction during transendothelial migration. J Cell Biol. 154:2001;147-160 Inhibition of RhoA or its kinase effector p160ROCK specifically inhibited monocyte tail retraction and caused accumulation of β2 integrins in the uropod. Whereas adhesion to ICAM-1 and VCAM-1 was significantly enhanced by p160ROCK inhibition, it was reduced by constitutively active p160ROCK.
    • (2001) J Cell Biol , vol.154 , pp. 147-160
    • Worthylake, R.A.1    Lemoine, S.2    Watson, J.M.3    Burridge, K.4
  • 81
    • 0038037737 scopus 로고    scopus 로고
    • RhoA and ROCK promote migration by limiting membrane protrusions
    • Worthylake R.A., Burridge K. RhoA and ROCK promote migration by limiting membrane protrusions. J Biol Chem. 278:2003;13578-13584.
    • (2003) J Biol Chem , vol.278 , pp. 13578-13584
    • Worthylake, R.A.1    Burridge, K.2
  • 82
    • 0036721793 scopus 로고    scopus 로고
    • Requirement for RhoA kinase activation in leukocyte de-adhesion
    • Liu L., Schwartz B.R., Lin N., Winn R.K., Harlan J.M. Requirement for RhoA kinase activation in leukocyte de-adhesion. J Immunol. 169:2002;2330-2336.
    • (2002) J Immunol , vol.169 , pp. 2330-2336
    • Liu, L.1    Schwartz, B.R.2    Lin, N.3    Winn, R.K.4    Harlan, J.M.5
  • 83
    • 0036180132 scopus 로고    scopus 로고
    • Interactions of integrins with their partner proteins in leukocyte membranes
    • Petty HR, Worth RG, Todd RFr: Interactions of integrins with their partner proteins in leukocyte membranes. Immunol Res 2002, 25:75-95.
    • (2002) Immunol Res , vol.25 , pp. 75-95
    • Petty, H.R.1    Worth, R.G.2    Todd, R.Fr.3
  • 84
    • 0038712496 scopus 로고    scopus 로고
    • Thrombospondin-bound integrin associated protein (CD47) physically and functionally modifies integrin αIIβ3 by its extracellular domain
    • A CD47-binding peptide derived from thrombospondin was shown to induce CD47-αIIbβ3 association and to promote binding of the ligand-mimetic antibody PAC1 to αIIbβ3. Intracellular signaling was not required for these effects, and a soluble extracellular fragment of CD47 was sufficient to mediate this activation.
    • Fujimoto T.T., Katsutani S., Shimomura T., Fujimura K. Thrombospondin-bound integrin associated protein (CD47) physically and functionally modifies integrin αIIβ3 by its extracellular domain. J Biol Chem. 278:2003;26655-26665 A CD47-binding peptide derived from thrombospondin was shown to induce CD47-αIIbβ3 association and to promote binding of the ligand-mimetic antibody PAC1 to αIIbβ3. Intracellular signaling was not required for these effects, and a soluble extracellular fragment of CD47 was sufficient to mediate this activation.
    • (2003) J Biol Chem , vol.278 , pp. 26655-26665
    • Fujimoto, T.T.1    Katsutani, S.2    Shimomura, T.3    Fujimura, K.4
  • 85
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand
    • By soaking a cyclic-RGD peptide ligand into a crystal of αVβ3 the details of the ligand-binding site are identified. While the aspartate sidechain coordinated to the metal in the MIDAS of the I-like domain of the β3 subunit, the arginine formed salt bridges with loops in blades 2 and 3 of the β-propeller domain of the αV subunit.
    • Xiong J.P., Stehle T., Zhang R., Joachimiak A., Frech M., Goodman S.L., Arnaout M.A. Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand. Science. 296: 2002;151-155 By soaking a cyclic-RGD peptide ligand into a crystal of αVβ3 the details of the ligand-binding site are identified. While the aspartate sidechain coordinated to the metal in the MIDAS of the I-like domain of the β3 subunit, the arginine formed salt bridges with loops in blades 2 and 3 of the β-propeller domain of the αV subunit.
    • (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
  • 86
    • 0026554716 scopus 로고
    • Regulation of locomotion and cell-cell contact area by the LFA-1 and ICAM-1 adhesion receptors
    • Dustin M.L., Carpen O., Springer T.A. Regulation of locomotion and cell-cell contact area by the LFA-1 and ICAM-1 adhesion receptors. J Immunol. 148:1992;2654-2663.
    • (1992) J Immunol , vol.148 , pp. 2654-2663
    • Dustin, M.L.1    Carpen, O.2    Springer, T.A.3


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