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Volumn 6, Issue , 2015, Pages

A RIAM/lamellipodin-talin-integrin complex forms the tip of sticky fingers that guide cell migration

Author keywords

[No Author keywords available]

Indexed keywords

ENHANCED GREEN FLUORESCENT PROTEIN; GLYCOPROTEIN; INTEGRIN; LAMELLIPODIN; TALIN; UNCLASSIFIED DRUG; VASODILATOR STIMULATED PHOSPHOPROTEIN; APBB1IP PROTEIN, HUMAN; CARRIER PROTEIN; MEMBRANE PROTEIN; PROTEIN BINDING; RAPH1 PROTEIN, HUMAN; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 84943190324     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms9492     Document Type: Article
Times cited : (69)

References (52)
  • 1
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard, T. D., Borisy, G. G. Cellular motility driven by assembly and disassembly of actin filaments. Cell 112, 453-465 (2003).
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 2
    • 34848927902 scopus 로고    scopus 로고
    • The many faces of actin: Matching assembly factors with cellular structures
    • Chhabra, E. S., Higgs, H. N. The many faces of actin: matching assembly factors with cellular structures. Nat. Cell Biol. 9, 1110-1121 (2007).
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1110-1121
    • Chhabra, E.S.1    Higgs, H.N.2
  • 3
    • 13944273671 scopus 로고    scopus 로고
    • Cell migration without a lamellipodium: Translation of actin dynamics into cell movement mediated by tropomyosin
    • Gupton, S. L. et al. Cell migration without a lamellipodium: translation of actin dynamics into cell movement mediated by tropomyosin. J. Cell Biol. 168, 619-631 (2005).
    • (2005) J. Cell Biol. , vol.168 , pp. 619-631
    • Gupton, S.L.1
  • 4
    • 84861926483 scopus 로고    scopus 로고
    • The Arp2/3 complex is required for lamellipodia extension and directional fibroblast cell migration
    • Suraneni, P. et al. The Arp2/3 complex is required for lamellipodia extension and directional fibroblast cell migration. J. Cell Biol. 197, 239-251 (2012).
    • (2012) J. Cell Biol. , vol.197 , pp. 239-251
    • Suraneni, P.1
  • 5
    • 44349179335 scopus 로고    scopus 로고
    • Filopodia: Molecular architecture and cellular functions
    • Mattila, P. K., Lappalainen, P. Filopodia: molecular architecture and cellular functions. Nat. Rev. Mol. Cell Biol. 9, 446-454 (2008).
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 446-454
    • Mattila, P.K.1    Lappalainen, P.2
  • 6
    • 36749024118 scopus 로고    scopus 로고
    • Filopodia: The fingers that do the walking
    • Gupton, S. L., Gertler, F. B. Filopodia: the fingers that do the walking. Sci. STKE 2007, re5 (2007).
    • (2007) Sci. STKE , vol.2007 , pp. re5
    • Gupton, S.L.1    Gertler, F.B.2
  • 7
  • 8
    • 0034745356 scopus 로고    scopus 로고
    • Rac recruits high-affinity integrin alphavbeta3 to lamellipodia in endothelial cell migration
    • Kiosses, W. B., Shattil, S. J., Pampori, N., Schwartz, M. A. Rac recruits high-affinity integrin alphavbeta3 to lamellipodia in endothelial cell migration. Nat. Cell Biol. 3, 316 (2001).
    • (2001) Nat. Cell Biol. , vol.3 , pp. 316
    • Kiosses, W.B.1    Shattil, S.J.2    Pampori, N.3    Schwartz, M.A.4
  • 9
    • 32644448252 scopus 로고    scopus 로고
    • The tumor suppressor DAPK inhibits cell motility by blocking the integrin-mediated polarity pathway
    • Kuo, J. C., Wang, W. J., Yao, C. C., Wu, P. R., Chen, R. H. The tumor suppressor DAPK inhibits cell motility by blocking the integrin-mediated polarity pathway. J. Cell Biol. 172, 619 (2006).
    • (2006) J. Cell Biol. , vol.172 , pp. 619
    • Kuo, J.C.1    Wang, W.J.2    Yao, C.C.3    Wu, P.R.4    Chen, R.H.5
  • 10
    • 33847159264 scopus 로고    scopus 로고
    • Polymerizing actin fibers position integrins primed to probe for adhesion sites
    • Galbraith, C. G., Yamada, K. M., Galbraith, J. A. Polymerizing actin fibers position integrins primed to probe for adhesion sites. Science 315, 992-995 (2007).
    • (2007) Science , vol.315 , pp. 992-995
    • Galbraith, C.G.1    Yamada, K.M.2    Galbraith, J.A.3
  • 11
    • 0141865705 scopus 로고    scopus 로고
    • Talin binding to integrin beta tails: A final common step in integrin activation
    • Tadokoro, S. et al. Talin binding to integrin beta tails: a final common step in integrin activation. Science 302, 103-106 (2003).
    • (2003) Science , vol.302 , pp. 103-106
    • Tadokoro, S.1
  • 12
    • 75749154495 scopus 로고    scopus 로고
    • Recreation of the terminal events in physiological integrin activation
    • Ye, F. et al. Recreation of the terminal events in physiological integrin activation. J. Cell Biol. 188, 157-173 (2010).
    • (2010) J. Cell Biol. , vol.188 , pp. 157-173
    • Ye, F.1
  • 13
    • 84857690534 scopus 로고    scopus 로고
    • The structure of cell-matrix adhesions: The new frontier
    • Hanein, D., Horwitz, A. R. The structure of cell-matrix adhesions: the new frontier. Curr. Opin. Cell Biol. 24, 134-140 (2012).
    • (2012) Curr. Opin. Cell Biol. , vol.24 , pp. 134-140
    • Hanein, D.1    Horwitz, A.R.2
  • 16
    • 15044359236 scopus 로고    scopus 로고
    • Linking Rap to cell adhesion
    • Bos, J. L. Linking Rap to cell adhesion. Curr. Opin. Cell Biol. 17, 123-128 (2005).
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 123-128
    • Bos, J.L.1
  • 17
    • 5044241734 scopus 로고    scopus 로고
    • RIAM, an Ena/VASP and Profilin ligand, interacts with Rap1-GTP and mediates Rap1-induced adhesion
    • Lafuente, E. M. et al. RIAM, an Ena/VASP and Profilin ligand, interacts with Rap1-GTP and mediates Rap1-induced adhesion. Dev. Cell 7, 585-595 (2004).
    • (2004) Dev. Cell , vol.7 , pp. 585-595
    • Lafuente, E.M.1
  • 18
    • 77949878456 scopus 로고    scopus 로고
    • G protein betagamma subunits regulate cell adhesion through Rap1a and its effector Radil
    • Ahmed, S. M., Daulat, A. M., Meunier, A., Angers, S. G protein betagamma subunits regulate cell adhesion through Rap1a and its effector Radil. J. Biol. Chem. 285, 6538-6551 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 6538-6551
    • Ahmed, S.M.1    Daulat, A.M.2    Meunier, A.3    Angers, S.4
  • 19
    • 84867401725 scopus 로고    scopus 로고
    • The MRL proteins: Adapting cell adhesion, migration and growth
    • Colo, G. P., Lafuente, E. M., Teixido, J. The MRL proteins: adapting cell adhesion, migration and growth. Eur. J. Cell Biol. 91, 861-868 (2012).
    • (2012) Eur. J. Cell Biol. , vol.91 , pp. 861-868
    • Colo, G.P.1    Lafuente, E.M.2    Teixido, J.3
  • 20
    • 5044244482 scopus 로고    scopus 로고
    • Lamellipodin, an Ena/VASP ligand, is implicated in the regulation of lamellipodial dynamics
    • Krause, M. et al. Lamellipodin, an Ena/VASP ligand, is implicated in the regulation of lamellipodial dynamics. Dev. Cell 7, 571-583 (2004).
    • (2004) Dev. Cell , vol.7 , pp. 571-583
    • Krause, M.1
  • 21
    • 84890138104 scopus 로고    scopus 로고
    • Lamellipodin and the Scar/WAVE complex cooperate to promote cell migration in vivo
    • Law, A. L. et al. Lamellipodin and the Scar/WAVE complex cooperate to promote cell migration in vivo. J. Cell Biol. 203, 673-689 (2013).
    • (2013) J. Cell Biol. , vol.203 , pp. 673-689
    • Law, A.L.1
  • 22
    • 33748454742 scopus 로고    scopus 로고
    • Reconstructing and deconstructing agonist-induced activation of integrin alphaIIbbeta3
    • Han, J. et al. Reconstructing and deconstructing agonist-induced activation of integrin alphaIIbbeta3. Curr. Biol. 16, 1796-1806 (2006).
    • (2006) Curr. Biol. , vol.16 , pp. 1796-1806
    • Han, J.1
  • 23
    • 84877157661 scopus 로고    scopus 로고
    • Two modes of integrin activation form a binary molecular switch in adhesion maturation
    • Lee, H. S., Anekal, P., Lim, C. J., Liu, C. C., Ginsberg, M. H. Two modes of integrin activation form a binary molecular switch in adhesion maturation. Mol. Biol. Cell 24, 1354-1362 (2013).
    • (2013) Mol. Biol. Cell , vol.24 , pp. 1354-1362
    • Lee, H.S.1    Anekal, P.2    Lim, C.J.3    Liu, C.C.4    Ginsberg, M.H.5
  • 24
    • 64149100431 scopus 로고    scopus 로고
    • RIAM activates integrins by linking talin to ras GTPase membrane-targeting sequences
    • Lee, H. S., Lim, C. J., Puzon-McLaughlin, W., Shattil, S. J., Ginsberg, M. H. RIAM activates integrins by linking talin to ras GTPase membrane-targeting sequences. J. Biol. Chem. 284, 5119-5127 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 5119-5127
    • Lee, H.S.1    Lim, C.J.2    Puzon-McLaughlin, W.3    Shattil, S.J.4    Ginsberg, M.H.5
  • 25
    • 33646198551 scopus 로고    scopus 로고
    • MIG-10/lamellipodin and AGE-1/PI3K promote axon guidance and outgrowth in response to slit and netrin
    • Chang, C. et al. MIG-10/lamellipodin and AGE-1/PI3K promote axon guidance and outgrowth in response to slit and netrin. Curr. Biol. 16, 854-862 (2006).
    • (2006) Curr. Biol. , vol.16 , pp. 854-862
    • Chang, C.1
  • 27
    • 48849113525 scopus 로고    scopus 로고
    • Visualization of protein interactions in living cells using bimolecular fluorescence complementation (BiFC) analysis
    • Chapter 21 Unit 21.3
    • Hu, C. D., Grinberg, A. V., Kerppola, T. K. Visualization of protein interactions in living cells using bimolecular fluorescence complementation (BiFC) analysis. Curr. Protoc. Cell Biol. Chapter 21, Unit 21.3 (2005).
    • (2005) Curr. Protoc. Cell Biol
    • Hu, C.D.1    Grinberg, A.V.2    Kerppola, T.K.3
  • 28
    • 34347222583 scopus 로고    scopus 로고
    • Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells
    • Kerppola, T. K. Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells. Nat. Protoc. 1, 1278-1286 (2006).
    • (2006) Nat. Protoc. , vol.1 , pp. 1278-1286
    • Kerppola, T.K.1
  • 29
    • 46249118002 scopus 로고    scopus 로고
    • Lifeact: A versatile marker to visualize F-actin
    • Riedl, J. et al. Lifeact: a versatile marker to visualize F-actin. Nat. Methods 5, 605-607 (2008).
    • (2008) Nat. Methods , vol.5 , pp. 605-607
    • Riedl, J.1
  • 30
    • 84856777960 scopus 로고    scopus 로고
    • Myosin-X: A MyTH-FERM myosin at the tips of filopodia
    • Kerber, M. L., Cheney, R. E. Myosin-X: a MyTH-FERM myosin at the tips of filopodia. J. Cell Sci. 124, 3733-3741 (2011).
    • (2011) J. Cell Sci. , vol.124 , pp. 3733-3741
    • Kerber, M.L.1    Cheney, R.E.2
  • 31
    • 84875439033 scopus 로고    scopus 로고
    • RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover
    • Goult, B. T. et al. RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover. J. Biol. Chem. 288, 8238-8249 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 8238-8249
    • Goult, B.T.1
  • 32
    • 84872049458 scopus 로고    scopus 로고
    • Fluorescence fluctuation approaches to the study of adhesion and signaling
    • Bachir, A. I., Kubow, K. E., Horwitz, A. R. Fluorescence fluctuation approaches to the study of adhesion and signaling. Methods Enzymol. 519, 167-201 (2013).
    • (2013) Methods Enzymol. , vol.519 , pp. 167-201
    • Bachir, A.I.1    Kubow, K.E.2    Horwitz, A.R.3
  • 33
    • 84906314998 scopus 로고    scopus 로고
    • Integrin-associated complexes form hierarchically with variable stoichiometry in nascent adhesions
    • Bachir, A. I. et al. Integrin-associated complexes form hierarchically with variable stoichiometry in nascent adhesions. Curr. Biol. 24, 1845-1853 (2014).
    • (2014) Curr. Biol. , vol.24 , pp. 1845-1853
    • Bachir, A.I.1
  • 34
    • 0030909050 scopus 로고    scopus 로고
    • Suppression of integrin activation: A novel function of a Ras/Raf-initiated MAP kinase pathway
    • Hughes, P. E. et al. Suppression of integrin activation: a novel function of a Ras/Raf-initiated MAP kinase pathway. Cell 88, 521 (1997).
    • (1997) Cell , vol.88 , pp. 521
    • Hughes, P.E.1
  • 35
    • 0022180156 scopus 로고
    • Changes in the platelet membrane glycoprotein IIb.IIIa complex during platelet activation
    • Shattil, S. J., Hoxie, J. A., Cunningham, M., Brass, L. F. Changes in the platelet membrane glycoprotein IIb.IIIa complex during platelet activation. J. Biol. Chem. 260, 11107-11114 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 11107-11114
    • Shattil, S.J.1    Hoxie, J.A.2    Cunningham, M.3    Brass, L.F.4
  • 36
    • 0025241904 scopus 로고
    • Selective inhibition of integrin function by antibodies specific for ligand-occupied receptor conformers
    • Frelinger, 3rd A. L. et al. Selective inhibition of integrin function by antibodies specific for ligand-occupied receptor conformers. J. Biol. Chem. 265, 6346-6352 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 6346-6352
    • Frelinger Iiia., L.1
  • 37
    • 0025873010 scopus 로고
    • Ligands activate" integrin alpha IIb beta3 (platelet GPIIb-IIIa)
    • Du, X. et al. Ligands "activate" integrin alpha IIb beta3 (platelet GPIIb-IIIa). Cell 65, 409 (1991).
    • (1991) Cell , vol.65 , pp. 409
    • Du, X.1
  • 38
    • 46249121793 scopus 로고    scopus 로고
    • Mechanisms and consequences of agonist-induced talin recruitment to platelet integrin alphaIIbbeta3
    • Watanabe, N. et al. Mechanisms and consequences of agonist-induced talin recruitment to platelet integrin alphaIIbbeta3. J. Cell Biol. 181, 1211-1222 (2008).
    • (2008) J. Cell Biol. , vol.181 , pp. 1211-1222
    • Watanabe, N.1
  • 40
    • 0025062149 scopus 로고
    • A beta 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation
    • Loftus, J. C. et al. A beta 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation. Science 249, 915-918 (1990).
    • (1990) Science , vol.249 , pp. 915-918
    • Loftus, J.C.1
  • 41
    • 33745785300 scopus 로고    scopus 로고
    • Visualization of molecular interactions by fluorescence complementation
    • Kerppola, T. K. Visualization of molecular interactions by fluorescence complementation. Nat Rev. Mol. Cell Biol. 7, 449-456 (2006).
    • (2006) Nat Rev. Mol. Cell Biol. , vol.7 , pp. 449-456
    • Kerppola, T.K.1
  • 42
    • 0035384692 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer microscopy: A mini review
    • Periasamy, A. Fluorescence resonance energy transfer microscopy: a mini review. J. Biomed. Optics 6, 287-291 (2001).
    • (2001) J. Biomed. Optics , vol.6 , pp. 287-291
    • Periasamy, A.1
  • 43
    • 84884814050 scopus 로고    scopus 로고
    • Structural studies on full-length talin1 reveal a compact auto-inhibited dimer: Implications for talin activation
    • Goult, B. T. et al. Structural studies on full-length talin1 reveal a compact auto-inhibited dimer: implications for talin activation. J. Struct. Biol. 184, 21-32 (2013).
    • (2013) J. Struct. Biol. , vol.184 , pp. 21-32
    • Goult, B.T.1
  • 44
    • 79957884622 scopus 로고    scopus 로고
    • Protein kinase A governs a RhoA-RhoGDI protrusionretraction pacemaker in migrating cells
    • Tkachenko, E. et al. Protein kinase A governs a RhoA-RhoGDI protrusionretraction pacemaker in migrating cells. Nat. Cell Biol. 13, 660-667 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 660-667
    • Tkachenko, E.1
  • 45
    • 51049104617 scopus 로고    scopus 로고
    • Actin and alpha-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner
    • Choi, C. K. et al. Actin and alpha-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner. Nat. Cell Biol. 10, 1039-1050 (2008).
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1039-1050
    • Choi, C.K.1
  • 46
    • 0025874695 scopus 로고
    • Accumulation of talin in nodes at the edge of the lamellipodium and separate incorporation into adhesion plaques at focal contacts in fibroblasts
    • DePasquale, J. A., Izzard, C. S. Accumulation of talin in nodes at the edge of the lamellipodium and separate incorporation into adhesion plaques at focal contacts in fibroblasts. J. Cell Biol. 113, 1351-1359 (1991).
    • (1991) J. Cell Biol. , vol.113 , pp. 1351-1359
    • DePasquale, J.A.1    Izzard, C.S.2
  • 47
    • 0023110249 scopus 로고
    • Induction of the fibrinogen receptor on human platelets by intracellular mediators
    • Shattil, S. J., Brass, L. F. Induction of the fibrinogen receptor on human platelets by intracellular mediators. J. Biol. Chem. 262, 992-1000 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 992-1000
    • Shattil, S.J.1    Brass, L.F.2
  • 49
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu, C. D., Chinenov, Y., Kerppola, T. K. Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell 9, 789-798 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 789-798
    • Hu, C.D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 50
    • 0035856483 scopus 로고    scopus 로고
    • Activation of Syk protein tyrosine kinase through interaction with integrin beta cytoplasmic domains
    • Woodside, D. G. et al. Activation of Syk protein tyrosine kinase through interaction with integrin beta cytoplasmic domains. Curr. Biol. 22, 1799 (2001).
    • (2001) Curr. Biol. , vol.22 , pp. 1799
    • Woodside, D.G.1
  • 51
    • 33748454742 scopus 로고    scopus 로고
    • Reconstructing and deconstructing agonist-induced activation of Integrin alphaIIbbeta3
    • Han, J. et al. Reconstructing and deconstructing agonist-induced activation of Integrin alphaIIbbeta3. Curr. Biol. 16, 1796 (2006).
    • (2006) Curr. Biol. , vol.16 , pp. 1796
    • Han, J.1
  • 52
    • 33645796494 scopus 로고    scopus 로고
    • Morphodynamic profiling of protrusion phenotypes
    • Machacek, M., Danuser, G. Morphodynamic profiling of protrusion phenotypes. Biophys. J. 90, 1439-1452 (2006).
    • (2006) Biophys. J. , vol.90 , pp. 1439-1452
    • Machacek, M.1    Danuser, G.2


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