메뉴 건너뛰기




Volumn 343, Issue 1, 2016, Pages 35-41

Mechanosensing in cell-matrix adhesions - Converting tension into chemical signals

Author keywords

Conformation; FAK; Fibronectin; Integrin; Paxillin; Talin

Indexed keywords

FIBRONECTIN; PAXILLIN; PROTEIN TYROSINE KINASE; TALIN;

EID: 84960857437     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2015.10.027     Document Type: Review
Times cited : (75)

References (64)
  • 1
    • 0033917881 scopus 로고    scopus 로고
    • Cell movement is guided by the rigidity of the substrate
    • Lo C.M., Wang H.B., Dembo M., Wang Y.L. Cell movement is guided by the rigidity of the substrate. Biophys. J. 2000, 79:144-152.
    • (2000) Biophys. J. , vol.79 , pp. 144-152
    • Lo, C.M.1    Wang, H.B.2    Dembo, M.3    Wang, Y.L.4
  • 3
    • 0035844869 scopus 로고    scopus 로고
    • Focal contacts as mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK- independent mechanism
    • Riveline D., Zamir E., Balaban N.Q., Schwarz U.S., Ishizaki T., Narumiya S., Kam Z., Geiger B., Bershadsky A.D. Focal contacts as mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK- independent mechanism. J. Cell Biol. 2001, 153:1175-1186.
    • (2001) J. Cell Biol. , vol.153 , pp. 1175-1186
    • Riveline, D.1    Zamir, E.2    Balaban, N.Q.3    Schwarz, U.S.4    Ishizaki, T.5    Narumiya, S.6    Kam, Z.7    Geiger, B.8    Bershadsky, A.D.9
  • 4
    • 84924692182 scopus 로고    scopus 로고
    • Competition between cap and basal actin fiber orientation in cells subjected to contact guidance and cyclic strain
    • Tamiello C., Bouten C.V., Baaijens F.P. Competition between cap and basal actin fiber orientation in cells subjected to contact guidance and cyclic strain. Sci. Rep. 2015, 5:8752.
    • (2015) Sci. Rep. , vol.5 , pp. 8752
    • Tamiello, C.1    Bouten, C.V.2    Baaijens, F.P.3
  • 5
    • 0035801529 scopus 로고    scopus 로고
    • Activation of integrins in endothelial cells by fluid shear stress mediates Rho-dependent cytoskeletal alignment
    • Tzima E., del Pozo M.A., Shattil S.J., Chien S., Schwartz M.A. Activation of integrins in endothelial cells by fluid shear stress mediates Rho-dependent cytoskeletal alignment. EMBO J. 2001, 20:4639-4647.
    • (2001) EMBO J. , vol.20 , pp. 4639-4647
    • Tzima, E.1    del Pozo, M.A.2    Shattil, S.J.3    Chien, S.4    Schwartz, M.A.5
  • 6
    • 77951728146 scopus 로고    scopus 로고
    • Pericellular fibronectin is required for RhoA-dependent responses to cyclic strain in fibroblasts
    • Lutz R., Sakai T., Chiquet M. Pericellular fibronectin is required for RhoA-dependent responses to cyclic strain in fibroblasts. J. Cell. Sci. 2010, 123:1511-1521.
    • (2010) J. Cell. Sci. , vol.123 , pp. 1511-1521
    • Lutz, R.1    Sakai, T.2    Chiquet, M.3
  • 12
    • 79551657030 scopus 로고    scopus 로고
    • Distinct roles for paxillin and Hic-5 in regulating breast cancer cell morphology, invasion, and metastasis
    • Deakin N.O., Turner C.E. Distinct roles for paxillin and Hic-5 in regulating breast cancer cell morphology, invasion, and metastasis. Mol. Biol. Cell. 2011, 22:327-341.
    • (2011) Mol. Biol. Cell. , vol.22 , pp. 327-341
    • Deakin, N.O.1    Turner, C.E.2
  • 13
    • 84928008693 scopus 로고    scopus 로고
    • Intravital imaging reveals how BRAF inhibition generates drug-tolerant microenvironments with high integrin beta1/FAK signaling
    • Hirata E., Girotti M.R., Viros A., Hooper S., Spencer-Dene B., Matsuda M., Larkin J., Marais R., Sahai E. Intravital imaging reveals how BRAF inhibition generates drug-tolerant microenvironments with high integrin beta1/FAK signaling. Cancer Cell 2015, 27:574-588.
    • (2015) Cancer Cell , vol.27 , pp. 574-588
    • Hirata, E.1    Girotti, M.R.2    Viros, A.3    Hooper, S.4    Spencer-Dene, B.5    Matsuda, M.6    Larkin, J.7    Marais, R.8    Sahai, E.9
  • 15
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix--cytoskeleton crosstalk
    • Geiger B., Bershadsky A., Pankov R., Yamada K.M. Transmembrane crosstalk between the extracellular matrix--cytoskeleton crosstalk. Nat. Rev. Mol. Cell. Biol. 2001, 2:793-805.
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.M.4
  • 17
    • 33847354235 scopus 로고    scopus 로고
    • Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells
    • Vicente-Manzanares M., Zareno J., Whitmore L., Choi C.K., Horwitz A.F. Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells. J. Cell Biol. 2007, 176:573-580.
    • (2007) J. Cell Biol. , vol.176 , pp. 573-580
    • Vicente-Manzanares, M.1    Zareno, J.2    Whitmore, L.3    Choi, C.K.4    Horwitz, A.F.5
  • 18
    • 0037128202 scopus 로고    scopus 로고
    • Force transduction by Triton cytoskeletons
    • Sawada Y., Sheetz M.P. Force transduction by Triton cytoskeletons. J. Cell Biol. 2002, 156:609-615.
    • (2002) J. Cell Biol. , vol.156 , pp. 609-615
    • Sawada, Y.1    Sheetz, M.P.2
  • 19
    • 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., Fassler 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    Fassler, R.4
  • 22
    • 33747152561 scopus 로고    scopus 로고
    • Matrix elasticity directs stem cell lineage specification
    • Engler A.J., Sen S., Sweeney H.L., Discher D.E. Matrix elasticity directs stem cell lineage specification. Cell 2006, 126:677-689.
    • (2006) Cell , vol.126 , pp. 677-689
    • Engler, A.J.1    Sen, S.2    Sweeney, H.L.3    Discher, D.E.4
  • 23
    • 1842426730 scopus 로고    scopus 로고
    • Cell shape, cytoskeletal tension, and RhoA regulate stem cell lineage commitment
    • McBeath R., Pirone D.M., Nelson C.M., Bhadriraju K., Chen C.S. Cell shape, cytoskeletal tension, and RhoA regulate stem cell lineage commitment. Dev. Cell 2004, 6:483-495.
    • (2004) Dev. Cell , vol.6 , pp. 483-495
    • McBeath, R.1    Pirone, D.M.2    Nelson, C.M.3    Bhadriraju, K.4    Chen, C.S.5
  • 25
    • 79955516270 scopus 로고    scopus 로고
    • Myosin IIA/IIB restrict adhesive and protrusive signaling to generate front-back polarity in migrating cells
    • Vicente-Manzanares M., Newell-Litwa K., Bachir A.I., Whitmore L.A., Horwitz A.R. Myosin IIA/IIB restrict adhesive and protrusive signaling to generate front-back polarity in migrating cells. J. Cell Biol. 2011, 193:381-396.
    • (2011) J. Cell Biol. , vol.193 , pp. 381-396
    • Vicente-Manzanares, M.1    Newell-Litwa, K.2    Bachir, A.I.3    Whitmore, L.A.4    Horwitz, A.R.5
  • 26
    • 79551678536 scopus 로고    scopus 로고
    • Cross-correlated fluctuation analysis reveals phosphorylation-regulated paxillin-FAK complexes in nascent adhesions
    • Choi C.K., Zareno J., Digman M.A., Gratton E., Horwitz A.R. Cross-correlated fluctuation analysis reveals phosphorylation-regulated paxillin-FAK complexes in nascent adhesions. Biophys. J. 2011, 100:583-592.
    • (2011) Biophys. J. , vol.100 , pp. 583-592
    • Choi, C.K.1    Zareno, J.2    Digman, M.A.3    Gratton, E.4    Horwitz, A.R.5
  • 30
    • 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. 2009, 284:5119-5127.
    • (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
  • 31
    • 46149093439 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of talin in regulating integrin activation
    • Goksoy E., Ma Y.Q., Wang X., Kong X., Perera D., Plow E.F., Qin J. Structural basis for the autoinhibition of talin in regulating integrin activation. Mol. Cell 2008, 31:124-133.
    • (2008) Mol. Cell , vol.31 , pp. 124-133
    • Goksoy, E.1    Ma, Y.Q.2    Wang, X.3    Kong, X.4    Perera, D.5    Plow, E.F.6    Qin, J.7
  • 33
    • 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., Sheetz M.P. Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin. Nature 2003, 424:334-337.
    • (2003) Nature , vol.424 , pp. 334-337
    • Jiang, G.1    Giannone, G.2    Critchley, D.R.3    Fukumoto, E.4    Sheetz, M.P.5
  • 35
    • 40149107045 scopus 로고    scopus 로고
    • How force might activate talin's vinculin binding sites: SMD reveals a structural mechanism
    • Hytonen V.P., Vogel V. How force might activate talin's vinculin binding sites: SMD reveals a structural mechanism. Plos Comput. Biol. 2008, 4:e24.
    • (2008) Plos Comput. Biol. , vol.4 , pp. e24
    • Hytonen, V.P.1    Vogel, V.2
  • 36
    • 34249705346 scopus 로고    scopus 로고
    • Force-induced activation of talin and its possible role in focal adhesion mechanotransduction
    • Lee S.E., Kamm R.D., Mofrad M.R. Force-induced activation of talin and its possible role in focal adhesion mechanotransduction. J. Biomech. 2007, 40:2096-2106.
    • (2007) J. Biomech. , vol.40 , pp. 2096-2106
    • Lee, S.E.1    Kamm, R.D.2    Mofrad, M.R.3
  • 38
    • 84855163922 scopus 로고    scopus 로고
    • Mechanotransduction in vivo by repeated talin stretch-relaxation events depends upon vinculin
    • Margadant F., Chew L.L., Hu X., Yu H., Bate N., Zhang X., Sheetz M. Mechanotransduction in vivo by repeated talin stretch-relaxation events depends upon vinculin. Plos Biol. 2011, 9:e1001223.
    • (2011) Plos Biol. , vol.9
    • Margadant, F.1    Chew, L.L.2    Hu, X.3    Yu, H.4    Bate, N.5    Zhang, X.6    Sheetz, M.7
  • 40
    • 0037117522 scopus 로고    scopus 로고
    • Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension
    • Baneyx G., Baugh L., Vogel V. Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension. Proc. Natl. Acad. Sci. USA 2002, 99:5139-5143.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5139-5143
    • Baneyx, G.1    Baugh, L.2    Vogel, V.3
  • 41
    • 80053434774 scopus 로고    scopus 로고
    • Intact alphaIIbbeta3 integrin is extended after activation as measured by solution X-ray scattering and electron microscopy
    • Eng E.T., Smagghe B.J., Walz T., Springer T.A. Intact alphaIIbbeta3 integrin is extended after activation as measured by solution X-ray scattering and electron microscopy. J. Biol. Chem. 2011, 286:35218-35226.
    • (2011) J. Biol. Chem. , vol.286 , pp. 35218-35226
    • Eng, E.T.1    Smagghe, B.J.2    Walz, T.3    Springer, T.A.4
  • 44
    • 57749116060 scopus 로고    scopus 로고
    • Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces
    • Zhu J., Luo B.H., Xiao T., Zhang C., Nishida N., Springer T.A. Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces. Mol. Cell 2008, 32:849-861.
    • (2008) Mol. Cell , vol.32 , pp. 849-861
    • Zhu, J.1    Luo, B.H.2    Xiao, T.3    Zhang, C.4    Nishida, N.5    Springer, T.A.6
  • 45
    • 84880008208 scopus 로고    scopus 로고
    • Complete integrin headpiece opening in eight steps
    • Zhu J., Zhu J., Springer T.A. Complete integrin headpiece opening in eight steps. J. Cell Biol. 2013, 201:1053-1068.
    • (2013) J. Cell Biol. , vol.201 , pp. 1053-1068
    • Zhu, J.1    Zhu, J.2    Springer, T.A.3
  • 46
    • 67649598285 scopus 로고    scopus 로고
    • Demonstration of catch bonds between an integrin and its ligand
    • Kong F., Garcia 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    Garcia, A.J.2    Mould, A.P.3    Humphries, M.J.4    Zhu, C.5
  • 47
    • 43149085289 scopus 로고    scopus 로고
    • Kindlin-2 (Mig-2): a co-activator of beta3 integrins
    • Ma Y.Q., Qin J., Wu C., Plow E.F. Kindlin-2 (Mig-2): a co-activator of beta3 integrins. J. Cell Biol. 2008, 181:439-446.
    • (2008) J. Cell Biol. , vol.181 , pp. 439-446
    • Ma, Y.Q.1    Qin, J.2    Wu, C.3    Plow, E.F.4
  • 48
    • 84946599583 scopus 로고    scopus 로고
    • The structure of a full-length membrane-embedded integrin bound to a physiological ligand
    • Dai A., Ye F., Taylor D.W., Hu G., Ginsberg M.H., Taylor K.A. The structure of a full-length membrane-embedded integrin bound to a physiological ligand. J. Biol. Chem. 2015.
    • (2015) J. Biol. Chem.
    • Dai, A.1    Ye, F.2    Taylor, D.W.3    Hu, G.4    Ginsberg, M.H.5    Taylor, K.A.6
  • 50
    • 50249107474 scopus 로고    scopus 로고
    • Paxillin comes of age
    • Deakin N.O., Turner C.E. Paxillin comes of age. J. Cell Sci. 2008, 121:2435-2444.
    • (2008) J. Cell Sci. , vol.121 , pp. 2435-2444
    • Deakin, N.O.1    Turner, C.E.2
  • 51
    • 0029827130 scopus 로고    scopus 로고
    • Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding
    • Brown M.C., Perrotta J.A., Turner C.E. Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding. J. Cell Biol. 1996, 135:1109-1123.
    • (1996) J. Cell Biol. , vol.135 , pp. 1109-1123
    • Brown, M.C.1    Perrotta, J.A.2    Turner, C.E.3
  • 52
    • 0028061406 scopus 로고
    • LIM domain recognition of a tyrosine-containing tight turn
    • Wu R.Y., Gill G.N. LIM domain recognition of a tyrosine-containing tight turn. J. Biol. Chem. 1994, 269:25085-25090.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25085-25090
    • Wu, R.Y.1    Gill, G.N.2
  • 53
    • 0029150292 scopus 로고
    • Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains
    • Schaller M.D., Otey C.A., Hildebrand J.D., Parsons J.T. Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains. J. Cell Biol. 1995, 130:1181-1187.
    • (1995) J. Cell Biol. , vol.130 , pp. 1181-1187
    • Schaller, M.D.1    Otey, C.A.2    Hildebrand, J.D.3    Parsons, J.T.4
  • 55
    • 40449133970 scopus 로고    scopus 로고
    • Kindlin-3 is essential for integrin activation and platelet aggregation
    • Moser M., Nieswandt B., Ussar S., Pozgajova M., Fassler R. Kindlin-3 is essential for integrin activation and platelet aggregation. Nat. Med. 2008, 14:325-330.
    • (2008) Nat. Med. , vol.14 , pp. 325-330
    • Moser, M.1    Nieswandt, B.2    Ussar, S.3    Pozgajova, M.4    Fassler, R.5
  • 56
    • 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., Eck M.J. Structural basis for the autoinhibition of focal adhesion kinase. Cell 2007, 129:1177-1187.
    • (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
  • 58
    • 77954351473 scopus 로고    scopus 로고
    • Knock-in mutation reveals an essential role for focal adhesion kinase activity in blood vessel morphogenesis and cell motility-polarity but not cell proliferation
    • Lim S.T., Chen X.L., Tomar A., Miller N.L., Yoo J., Schlaepfer D.D. Knock-in mutation reveals an essential role for focal adhesion kinase activity in blood vessel morphogenesis and cell motility-polarity but not cell proliferation. J. Biol. Chem. 2010, 285:21526-21536.
    • (2010) J. Biol. Chem. , vol.285 , pp. 21526-21536
    • Lim, S.T.1    Chen, X.L.2    Tomar, A.3    Miller, N.L.4    Yoo, J.5    Schlaepfer, D.D.6
  • 59
    • 0037107551 scopus 로고    scopus 로고
    • Fibronectin at a glance
    • Pankov R., Yamada K.M. Fibronectin at a glance. J. Cell Sci. 2002, 115:3861-3863.
    • (2002) J. Cell Sci. , vol.115 , pp. 3861-3863
    • Pankov, R.1    Yamada, K.M.2
  • 61
    • 1642493664 scopus 로고    scopus 로고
    • Tuning the mechanical stability of fibronectin type III modules through sequence variations
    • Craig D., Gao M., Schulten K., Vogel V. Tuning the mechanical stability of fibronectin type III modules through sequence variations. Structure 2004, 12:21-30.
    • (2004) Structure , vol.12 , pp. 21-30
    • Craig, D.1    Gao, M.2    Schulten, K.3    Vogel, V.4
  • 63
    • 84880260541 scopus 로고    scopus 로고
    • Stretching fibronectin fibres disrupts binding of bacterial adhesins by physically destroying an epitope
    • Chabria M., Hertig S., Smith M.L., Vogel V. Stretching fibronectin fibres disrupts binding of bacterial adhesins by physically destroying an epitope. Nat. Commun. 2010, 1:135.
    • (2010) Nat. Commun. , vol.1 , pp. 135
    • Chabria, M.1    Hertig, S.2    Smith, M.L.3    Vogel, V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.