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Volumn 14, Issue 11, 2016, Pages 2668-2682

IPP Complex Reinforces Adhesion by Relaying Tension-Dependent Signals to Inhibit Integrin Turnover

Author keywords

Endocytosis; Integrin linked kinase; Mechanosensing; Mechanotransduction

Indexed keywords

INTEGRIN; IPP COMPLEX; REGULATOR PROTEIN; UNCLASSIFIED DRUG; ACTIN; ACTIN BINDING PROTEIN; DROSOPHILA PROTEIN; INTEGRIN-LINKED KINASE; PARVIN PROTEIN, DROSOPHILA; PINCH PROTEIN, DROSOPHILA; PROTEIN BINDING; PROTEIN SERINE THREONINE KINASE; TALIN; TRANSCRIPTION FACTOR;

EID: 84959864235     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2016.02.052     Document Type: Article
Times cited : (13)

References (75)
  • 1
    • 84871712311 scopus 로고    scopus 로고
    • An integrin-ILK-microtubule network orients cell polarity and lumen formation in glandular epithelium
    • Akhtar N., Streuli C.H. An integrin-ILK-microtubule network orients cell polarity and lumen formation in glandular epithelium. Nat. Cell Biol. 2013, 15:17-27.
    • (2013) Nat. Cell Biol. , vol.15 , pp. 17-27
    • Akhtar, N.1    Streuli, C.H.2
  • 3
    • 0035945353 scopus 로고    scopus 로고
    • Marching at the front and dragging behind: differential alphaVbeta3-integrin turnover regulates focal adhesion behavior
    • Ballestrem C., Hinz B., Imhof B.A., Wehrle-Haller B. Marching at the front and dragging behind: differential alphaVbeta3-integrin turnover regulates focal adhesion behavior. J. Cell Biol. 2001, 155:1319-1332.
    • (2001) J. Cell Biol. , vol.155 , pp. 1319-1332
    • Ballestrem, C.1    Hinz, B.2    Imhof, B.A.3    Wehrle-Haller, B.4
  • 5
    • 0035891368 scopus 로고    scopus 로고
    • Zipper nonmuscle myosin-II functions downstream of PS2 integrin in Drosophila myogenesis and is necessary for myofibril formation
    • Bloor J.W., Kiehart D.P. Zipper nonmuscle myosin-II functions downstream of PS2 integrin in Drosophila myogenesis and is necessary for myofibril formation. Dev. Biol. 2001, 239:215-228.
    • (2001) Dev. Biol. , vol.239 , pp. 215-228
    • Bloor, J.W.1    Kiehart, D.P.2
  • 7
    • 0028173625 scopus 로고
    • PS integrin subunit genes have distinct phenotypes
    • PS integrin subunit genes have distinct phenotypes. Development 1994, 120:1221-1231.
    • (1994) Development , vol.120 , pp. 1221-1231
    • Brown, N.H.1
  • 9
    • 76249113509 scopus 로고    scopus 로고
    • Integrin alphaIIbbeta3 activation in Chinese hamster ovary cells and platelets increases clustering rather than affinity
    • Bunch T.A. Integrin alphaIIbbeta3 activation in Chinese hamster ovary cells and platelets increases clustering rather than affinity. J. Biol. Chem. 2010, 285:1841-1849.
    • (2010) J. Biol. Chem. , vol.285 , pp. 1841-1849
    • Bunch, T.A.1
  • 13
    • 0038409304 scopus 로고    scopus 로고
    • Analysis of PINCH function in Drosophila demonstrates its requirement in integrin-dependent cellular processes
    • Clark K.A., McGrail M., Beckerle M.C. Analysis of PINCH function in Drosophila demonstrates its requirement in integrin-dependent cellular processes. Development 2003, 130:2611-2621.
    • (2003) Development , vol.130 , pp. 2611-2621
    • Clark, K.A.1    McGrail, M.2    Beckerle, M.C.3
  • 14
    • 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., Wehrle-Haller B. The mechanisms and dynamics of (alpha)v(beta)3 integrin clustering in living cells. J. Cell Biol. 2005, 171:383-392.
    • (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
  • 16
    • 34547678544 scopus 로고    scopus 로고
    • Mutations in the Drosophila alphaPS2 integrin subunit uncover new features of adhesion site assembly
    • Devenport D., Bunch T.A., Bloor J.W., Brower D.L., Brown N.H. Mutations in the Drosophila alphaPS2 integrin subunit uncover new features of adhesion site assembly. Dev. Biol. 2007, 308:294-308.
    • (2007) Dev. Biol. , vol.308 , pp. 294-308
    • Devenport, D.1    Bunch, T.A.2    Bloor, J.W.3    Brower, D.L.4    Brown, N.H.5
  • 21
    • 59149097344 scopus 로고    scopus 로고
    • Mechanically activated integrin switch controls alpha5beta1 function
    • Friedland J.C., Lee M.H., Boettiger D. Mechanically activated integrin switch controls alpha5beta1 function. Science 2009, 323:642-644.
    • (2009) Science , vol.323 , pp. 642-644
    • Friedland, J.C.1    Lee, M.H.2    Boettiger, D.3
  • 22
    • 0037175402 scopus 로고    scopus 로고
    • The relationship between force and focal complex development
    • Galbraith C.G., Yamada K.M., Sheetz M.P. The relationship between force and focal complex development. J. Cell Biol. 2002, 159:695-705.
    • (2002) J. Cell Biol. , vol.159 , pp. 695-705
    • Galbraith, C.G.1    Yamada, K.M.2    Sheetz, M.P.3
  • 23
    • 84866881804 scopus 로고    scopus 로고
    • Mechanical feedback between membrane tension and dynamics
    • Gauthier N.C., Masters T.A., Sheetz M.P. Mechanical feedback between membrane tension and dynamics. Trends Cell Biol. 2012, 22:527-535.
    • (2012) Trends Cell Biol. , vol.22 , pp. 527-535
    • Gauthier, N.C.1    Masters, T.A.2    Sheetz, M.P.3
  • 25
    • 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., Sheetz M.P. Talin1 is critical for force-dependent reinforcement of initial integrin-cytoskeleton bonds but not tyrosine kinase activation. J. Cell Biol. 2003, 163:409-419.
    • (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
  • 26
    • 0034627831 scopus 로고    scopus 로고
    • Requirements of Kettin, a giant muscle protein highly conserved in overall structure in evolution, for normal muscle function, viability, and flight activity of Drosophila
    • Hakeda S., Endo S., Saigo K. Requirements of Kettin, a giant muscle protein highly conserved in overall structure in evolution, for normal muscle function, viability, and flight activity of Drosophila. J. Cell Biol. 2000, 148:101-114.
    • (2000) J. Cell Biol. , vol.148 , pp. 101-114
    • Hakeda, S.1    Endo, S.2    Saigo, K.3
  • 27
    • 84878324673 scopus 로고    scopus 로고
    • Forces in tissue morphogenesis and patterning
    • Heisenberg C.P., Bellaïche Y. Forces in tissue morphogenesis and patterning. Cell 2013, 153:948-962.
    • (2013) Cell , vol.153 , pp. 948-962
    • Heisenberg, C.P.1    Bellaïche, Y.2
  • 30
    • 78649738478 scopus 로고    scopus 로고
    • Caveolin limits membrane microdomain mobility and integrin-mediated uptake of fibronectin-binding pathogens
    • Hoffmann C., Berking A., Agerer F., Buntru A., Neske F., Chhatwal G.S., Ohlsen K., Hauck C.R. Caveolin limits membrane microdomain mobility and integrin-mediated uptake of fibronectin-binding pathogens. J. Cell Sci. 2010, 123:4280-4291.
    • (2010) J. Cell Sci. , vol.123 , pp. 4280-4291
    • Hoffmann, C.1    Berking, A.2    Agerer, F.3    Buntru, A.4    Neske, F.5    Chhatwal, G.S.6    Ohlsen, K.7    Hauck, C.R.8
  • 31
    • 84902665682 scopus 로고    scopus 로고
    • Symmetric exchange of multi-protein building blocks between stationary focal adhesions and the cytosol
    • Hoffmann J.E., Fermin Y., Stricker R.L., Ickstadt K., Zamir E. Symmetric exchange of multi-protein building blocks between stationary focal adhesions and the cytosol. eLife 2014, 3:e02257.
    • (2014) eLife , vol.3 , pp. e02257
    • Hoffmann, J.E.1    Fermin, Y.2    Stricker, R.L.3    Ickstadt, K.4    Zamir, E.5
  • 33
    • 84893238618 scopus 로고    scopus 로고
    • The integrin-linked kinase-PINCH-parvin complex supports integrin αIIbβ3 activation
    • Honda S., Shirotani-Ikejima H., Tadokoro S., Tomiyama Y., Miyata T. The integrin-linked kinase-PINCH-parvin complex supports integrin αIIbβ3 activation. PLoS ONE 2013, 8:e85498.
    • (2013) PLoS ONE , vol.8 , pp. e85498
    • Honda, S.1    Shirotani-Ikejima, H.2    Tadokoro, S.3    Tomiyama, Y.4    Miyata, T.5
  • 36
    • 3342958175 scopus 로고    scopus 로고
    • Identification of integrin beta subunit mutations that alter heterodimer function in situ
    • Jannuzi A.L., Bunch T.A., West R.F., Brower D.L. Identification of integrin beta subunit mutations that alter heterodimer function in situ. Mol. Biol. Cell 2004, 15:3829-3840.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3829-3840
    • Jannuzi, A.L.1    Bunch, T.A.2    West, R.F.3    Brower, D.L.4
  • 38
    • 80052187643 scopus 로고    scopus 로고
    • Identification of integrin beta subunit mutations that alter affinity for extracellular matrix ligand
    • Kendall T., Mukai L., Jannuzi A.L., Bunch T.A. Identification of integrin beta subunit mutations that alter affinity for extracellular matrix ligand. J. Biol. Chem. 2011, 286:30981-30993.
    • (2011) J. Biol. Chem. , vol.286 , pp. 30981-30993
    • Kendall, T.1    Mukai, L.2    Jannuzi, A.L.3    Bunch, T.A.4
  • 39
    • 84862598504 scopus 로고    scopus 로고
    • Talin activates integrins by altering the topology of the β transmembrane domain
    • Kim C., Ye F., Hu X., Ginsberg M.H. Talin activates integrins by altering the topology of the β transmembrane domain. J. Cell Biol. 2012, 197:605-611.
    • (2012) J. Cell Biol. , vol.197 , pp. 605-611
    • Kim, C.1    Ye, F.2    Hu, X.3    Ginsberg, M.H.4
  • 41
    • 70349614410 scopus 로고    scopus 로고
    • Integrin-linked kinase controls vascular wall formation by negatively regulating Rho/ROCK-mediated vascular smooth muscle cell contraction
    • Kogata N., Tribe R.M., Fässler R., Way M., Adams R.H. Integrin-linked kinase controls vascular wall formation by negatively regulating Rho/ROCK-mediated vascular smooth muscle cell contraction. Genes Dev. 2009, 23:2278-2283.
    • (2009) Genes Dev. , vol.23 , pp. 2278-2283
    • Kogata, N.1    Tribe, R.M.2    Fässler, R.3    Way, M.4    Adams, R.H.5
  • 42
    • 67649598285 scopus 로고    scopus 로고
    • Demonstration of catch bonds between an integrin and its ligand
    • Kong F., García A.J., Mould A.P., Humphries M.J., Zhu C. Demonstration of catch bonds between an integrin and its ligand. J. Cell Biol. 2009, 185:1275-1284.
    • (2009) J. Cell Biol. , vol.185 , pp. 1275-1284
    • Kong, F.1    García, A.J.2    Mould, A.P.3    Humphries, M.J.4    Zhu, C.5
  • 46
    • 84879421708 scopus 로고    scopus 로고
    • The effect of ligand affinity on integrins' lateral diffusion in cultured cells
    • Mainali D., Smith E.A. The effect of ligand affinity on integrins' lateral diffusion in cultured cells. Eur. Biophys. J. 2013, 42:281-290.
    • (2013) Eur. Biophys. J. , vol.42 , pp. 281-290
    • Mainali, D.1    Smith, E.A.2
  • 47
    • 0032759039 scopus 로고    scopus 로고
    • Directionality of wingless protein transport influences epidermal patterning in the Drosophila embryo
    • Moline M.M., Southern C., Bejsovec A. Directionality of wingless protein transport influences epidermal patterning in the Drosophila embryo. Development 1999, 126:4375-4384.
    • (1999) Development , vol.126 , pp. 4375-4384
    • Moline, M.M.1    Southern, C.2    Bejsovec, A.3
  • 48
    • 1842456978 scopus 로고    scopus 로고
    • Characterization of a hypercontraction-induced myopathy in Drosophila caused by mutations in Mhc
    • Montana E.S., Littleton J.T. Characterization of a hypercontraction-induced myopathy in Drosophila caused by mutations in Mhc. J. Cell Biol. 2004, 164:1045-1054.
    • (2004) J. Cell Biol. , vol.164 , pp. 1045-1054
    • Montana, E.S.1    Littleton, J.T.2
  • 49
    • 70350345546 scopus 로고    scopus 로고
    • Alpha-parvin controls vascular mural cell recruitment to vessel wall by regulating RhoA/ROCK signalling
    • Montanez E., Wickström S.A., Altstätter J., Chu H., Fässler R. Alpha-parvin controls vascular mural cell recruitment to vessel wall by regulating RhoA/ROCK signalling. EMBO J. 2009, 28:3132-3144.
    • (2009) EMBO J. , vol.28 , pp. 3132-3144
    • Montanez, E.1    Wickström, S.A.2    Altstätter, J.3    Chu, H.4    Fässler, R.5
  • 50
    • 77955580383 scopus 로고    scopus 로고
    • Stretchy proteins on stretchy substrates: the important elements of integrin-mediated rigidity sensing
    • Moore S.W., Roca-Cusachs P., Sheetz M.P. Stretchy proteins on stretchy substrates: the important elements of integrin-mediated rigidity sensing. Dev. Cell 2010, 19:194-206.
    • (2010) Dev. Cell , vol.19 , pp. 194-206
    • Moore, S.W.1    Roca-Cusachs, P.2    Sheetz, M.P.3
  • 51
    • 0024230185 scopus 로고
    • Molecular and ultrastructural defects in a Drosophila myosin heavy chain mutant: differential effects on muscle function produced by similar thick filament abnormalities
    • O'Donnell P.T., Bernstein S.I. Molecular and ultrastructural defects in a Drosophila myosin heavy chain mutant: differential effects on muscle function produced by similar thick filament abnormalities. J. Cell Biol. 1988, 107:2601-2612.
    • (1988) J. Cell Biol. , vol.107 , pp. 2601-2612
    • O'Donnell, P.T.1    Bernstein, S.I.2
  • 53
    • 84875982576 scopus 로고    scopus 로고
    • Elevated expression of the integrin-associated protein PINCH suppresses the defects of Drosophila melanogaster muscle hypercontraction mutants
    • Pronovost S.M., Beckerle M.C., Kadrmas J.L. Elevated expression of the integrin-associated protein PINCH suppresses the defects of Drosophila melanogaster muscle hypercontraction mutants. PLoS Genet. 2013, 9:e1003406.
    • (2013) PLoS Genet. , vol.9 , pp. e1003406
    • Pronovost, S.M.1    Beckerle, M.C.2    Kadrmas, J.L.3
  • 55
    • 0033803415 scopus 로고    scopus 로고
    • Postsynaptic filopodia in muscle cells interact with innervating motoneuron axons
    • Ritzenthaler S., Suzuki E., Chiba A. Postsynaptic filopodia in muscle cells interact with innervating motoneuron axons. Nat. Neurosci. 2000, 3:1012-1017.
    • (2000) Nat. Neurosci. , vol.3 , pp. 1012-1017
    • Ritzenthaler, S.1    Suzuki, E.2    Chiba, A.3
  • 56
    • 84869102195 scopus 로고    scopus 로고
    • Finding the weakest link: exploring integrin-mediated mechanical molecular pathways
    • Roca-Cusachs P., Iskratsch T., Sheetz M.P. Finding the weakest link: exploring integrin-mediated mechanical molecular pathways. J. Cell Sci. 2012, 125:3025-3038.
    • (2012) J. Cell Sci. , vol.125 , pp. 3025-3038
    • Roca-Cusachs, P.1    Iskratsch, T.2    Sheetz, M.P.3
  • 59
    • 79952283069 scopus 로고    scopus 로고
    • Quantitative proteomics of the integrin adhesome show a myosin II-dependent recruitment of LIM domain proteins
    • Schiller H.B., Friedel C.C., Boulegue C., Fässler R. Quantitative proteomics of the integrin adhesome show a myosin II-dependent recruitment of LIM domain proteins. EMBO Rep. 2011, 12:259-266.
    • (2011) EMBO Rep. , vol.12 , pp. 259-266
    • Schiller, H.B.1    Friedel, C.C.2    Boulegue, C.3    Fässler, R.4
  • 62
    • 33646683097 scopus 로고    scopus 로고
    • Multiple factors contribute to integrin-talin interactions in vivo
    • Tanentzapf G., Martin-Bermudo M.D., Hicks M.S., Brown N.H. Multiple factors contribute to integrin-talin interactions in vivo. J. Cell Sci. 2006, 119:1632-1644.
    • (2006) J. Cell Sci. , vol.119 , pp. 1632-1644
    • Tanentzapf, G.1    Martin-Bermudo, M.D.2    Hicks, M.S.3    Brown, N.H.4
  • 63
    • 58149519189 scopus 로고    scopus 로고
    • CAP (Cbl associated protein) regulates receptor-mediated endocytosis
    • Tosoni D., Cestra G. CAP (Cbl associated protein) regulates receptor-mediated endocytosis. FEBS Lett. 2009, 583:293-300.
    • (2009) FEBS Lett. , vol.583 , pp. 293-300
    • Tosoni, D.1    Cestra, G.2
  • 65
    • 84867530808 scopus 로고    scopus 로고
    • Functional analysis of parvin and different modes of IPP-complex assembly at integrin sites during Drosophila development
    • Vakaloglou K.M., Chountala M., Zervas C.G. Functional analysis of parvin and different modes of IPP-complex assembly at integrin sites during Drosophila development. J. Cell Sci. 2012, 125:3221-3232.
    • (2012) J. Cell Sci. , vol.125 , pp. 3221-3232
    • Vakaloglou, K.M.1    Chountala, M.2    Zervas, C.G.3
  • 66
    • 37249092533 scopus 로고    scopus 로고
    • Analysis of integrin dynamics by fluorescence recovery after photobleaching
    • Wehrle-Haller B. Analysis of integrin dynamics by fluorescence recovery after photobleaching. Methods Mol. Biol. 2007, 370:173-202.
    • (2007) Methods Mol. Biol. , vol.370 , pp. 173-202
    • Wehrle-Haller, B.1
  • 67
    • 84866480296 scopus 로고    scopus 로고
    • A spatial model for integrin clustering as a result of feedback between integrin activation and integrin binding
    • Welf E.S., Naik U.P., Ogunnaike B.A. A spatial model for integrin clustering as a result of feedback between integrin activation and integrin binding. Biophys. J. 2012, 103:1379-1389.
    • (2012) Biophys. J. , vol.103 , pp. 1379-1389
    • Welf, E.S.1    Naik, U.P.2    Ogunnaike, B.A.3
  • 69
    • 79955538660 scopus 로고    scopus 로고
    • Actomyosin-generated tension controls the molecular kinetics of focal adhesions
    • Wolfenson H., Bershadsky A., Henis Y.I., Geiger B. Actomyosin-generated tension controls the molecular kinetics of focal adhesions. J. Cell Sci. 2011, 124:1425-1432.
    • (2011) J. Cell Sci. , vol.124 , pp. 1425-1432
    • Wolfenson, H.1    Bershadsky, A.2    Henis, Y.I.3    Geiger, B.4
  • 70
    • 84875273788 scopus 로고    scopus 로고
    • Dynamic regulation of the structure and functions of integrin adhesions
    • Wolfenson H., Lavelin I., Geiger B. Dynamic regulation of the structure and functions of integrin adhesions. Dev. Cell 2013, 24:447-458.
    • (2013) Dev. Cell , vol.24 , pp. 447-458
    • Wolfenson, H.1    Lavelin, I.2    Geiger, B.3
  • 71
    • 84898467976 scopus 로고    scopus 로고
    • Mechanical activation of vinculin binding to talin locks talin in an unfolded conformation
    • Yao M., Goult B.T., Chen H., Cong P., Sheetz M.P., Yan J. Mechanical activation of vinculin binding to talin locks talin in an unfolded conformation. Sci. Rep. 2014, 4:4610.
    • (2014) Sci. Rep. , vol.4 , pp. 4610
    • Yao, M.1    Goult, B.T.2    Chen, H.3    Cong, P.4    Sheetz, M.P.5    Yan, J.6
  • 73
    • 77951184233 scopus 로고    scopus 로고
    • Analysis of integrin turnover in fly myotendinous junctions
    • Yuan L., Fairchild M.J., Perkins A.D., Tanentzapf G. Analysis of integrin turnover in fly myotendinous junctions. J. Cell Sci. 2010, 123:939-946.
    • (2010) J. Cell Sci. , vol.123 , pp. 939-946
    • Yuan, L.1    Fairchild, M.J.2    Perkins, A.D.3    Tanentzapf, G.4
  • 74
    • 0035809918 scopus 로고    scopus 로고
    • Drosophila integrin-linked kinase is required at sites of integrin adhesion to link the cytoskeleton to the plasma membrane
    • Zervas C.G., Gregory S.L., Brown N.H. Drosophila integrin-linked kinase is required at sites of integrin adhesion to link the cytoskeleton to the plasma membrane. J. Cell Biol. 2001, 152:1007-1018.
    • (2001) J. Cell Biol. , vol.152 , pp. 1007-1018
    • Zervas, C.G.1    Gregory, S.L.2    Brown, N.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.