메뉴 건너뛰기




Volumn 5, Issue 5, 2013, Pages 1456-1468

Integrin-matrix clusters form podosome-like adhesions in the absence of traction forces

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN RELATED PROTEIN 2; ACTIN RELATED PROTEIN 3; ARAP3 PROTEIN; ARGININE; ASPARTIC ACID; CELL PROTEIN; F ACTIN; FAK PROTEIN; FOCAL ADHESION KINASE 2; GAP PROTEIN; GLASS; GLYCINE; INTEGRIN; MATRIX METALLOPROTEINASE; NEURAL WISKOTT ALDRICH SYNDROME PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; TRIPEPTIDE; UNCLASSIFIED DRUG;

EID: 84890180948     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2013.10.040     Document Type: Article
Times cited : (117)

References (67)
  • 1
    • 77950532162 scopus 로고    scopus 로고
    • Fusion of biomimetic stealth probes into lipid bilayer cores
    • Almquist B.D., Melosh N.A. Fusion of biomimetic stealth probes into lipid bilayer cores. Proc. Natl. Acad. Sci. USA 2010, 107:5815-5820.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 5815-5820
    • Almquist, B.D.1    Melosh, N.A.2
  • 2
    • 26444452643 scopus 로고    scopus 로고
    • Abl kinases regulate actin comet tail elongation via an N-WASP-dependent pathway
    • Burton E.A., Oliver T.N., Pendergast A.M. Abl kinases regulate actin comet tail elongation via an N-WASP-dependent pathway. Mol. Cell. Biol. 2005, 25:8834-8843.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8834-8843
    • Burton, E.A.1    Oliver, T.N.2    Pendergast, A.M.3
  • 3
    • 60749128399 scopus 로고    scopus 로고
    • Force propagation across cells: mechanical coherence of dynamic cytoskeletons
    • Cai Y., Sheetz M.P. Force propagation across cells: mechanical coherence of dynamic cytoskeletons. Curr. Opin. Cell Biol. 2009, 21:47-50.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 47-50
    • Cai, Y.1    Sheetz, M.P.2
  • 5
    • 0029979722 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase
    • Chen H.C., Appeddu P.A., Isoda H., Guan J.L. Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase. J.Biol. Chem. 1996, 271:26329-26334.
    • (1996) J.Biol. Chem. , vol.271 , pp. 26329-26334
    • Chen, H.C.1    Appeddu, P.A.2    Isoda, H.3    Guan, J.L.4
  • 7
    • 77956163491 scopus 로고    scopus 로고
    • Regulation of WASp by phosphorylation: Activation or other functions?
    • Dovas A., Cox D. Regulation of WASp by phosphorylation: Activation or other functions?. Commun. Integr. Biol. 2010, 3:101-105.
    • (2010) Commun. Integr. Biol. , vol.3 , pp. 101-105
    • Dovas, A.1    Cox, D.2
  • 8
    • 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
  • 9
    • 0028050160 scopus 로고
    • Hidden dynamics in rapid changes of bilayer shape
    • Evans E., Yeung A. Hidden dynamics in rapid changes of bilayer shape. Chem. Phys. Lipids 1994, 73:39-56.
    • (1994) Chem. Phys. Lipids , vol.73 , pp. 39-56
    • Evans, E.1    Yeung, A.2
  • 10
    • 0343604223 scopus 로고
    • Mechanochemical properties of membranes
    • Academic Press, New York, B. Felix, K. Arnost (Eds.)
    • Evans E.A., Hochmuth R.M. Mechanochemical properties of membranes. Current Topics in Membranes and Transport 1978, 1-64. Academic Press, New York. B. Felix, K. Arnost (Eds.).
    • (1978) Current Topics in Membranes and Transport , pp. 1-64
    • Evans, E.A.1    Hochmuth, R.M.2
  • 11
    • 0037512351 scopus 로고    scopus 로고
    • Macrophage podosomes assemble at the leading lamella by growth and fragmentation
    • Evans J.G., Correia I., Krasavina O., Watson N., Matsudaira P. Macrophage podosomes assemble at the leading lamella by growth and fragmentation. J.Cell Biol. 2003, 161:697-705.
    • (2003) J.Cell Biol. , vol.161 , pp. 697-705
    • Evans, J.G.1    Correia, I.2    Krasavina, O.3    Watson, N.4    Matsudaira, P.5
  • 14
    • 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
  • 20
    • 52649168924 scopus 로고    scopus 로고
    • Quantifying cell-matrix adhesion dynamics in living cells using interference reflection microscopy
    • Holt M.R., Calle Y., Sutton D.H., Critchley D.R., Jones G.E., Dunn G.A. Quantifying cell-matrix adhesion dynamics in living cells using interference reflection microscopy. J.Microsc. 2008, 232:73-81.
    • (2008) J.Microsc. , vol.232 , pp. 73-81
    • Holt, M.R.1    Calle, Y.2    Sutton, D.H.3    Critchley, D.R.4    Jones, G.E.5    Dunn, G.A.6
  • 24
    • 18244392475 scopus 로고    scopus 로고
    • Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices
    • Krugmann S., Anderson K.E., Ridley S.H., Risso N., McGregor A., Coadwell J., Davidson K., Eguinoa A., Ellson C.D., Lipp P., et al. Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices. Mol. Cell 2002, 9:95-108.
    • (2002) Mol. Cell , vol.9 , pp. 95-108
    • Krugmann, S.1    Anderson, K.E.2    Ridley, S.H.3    Risso, N.4    McGregor, A.5    Coadwell, J.6    Davidson, K.7    Eguinoa, A.8    Ellson, C.D.9    Lipp, P.10
  • 26
    • 79956139704 scopus 로고    scopus 로고
    • The guanine nucleotide exchange factor Arhgef5 plays crucial roles in Src-induced podosome formation
    • Kuroiwa M., Oneyama C., Nada S., Okada M. The guanine nucleotide exchange factor Arhgef5 plays crucial roles in Src-induced podosome formation. J.Cell Sci. 2011, 124:1726-1738.
    • (2011) J.Cell Sci. , vol.124 , pp. 1726-1738
    • Kuroiwa, M.1    Oneyama, C.2    Nada, S.3    Okada, M.4
  • 28
    • 21044433334 scopus 로고    scopus 로고
    • Podosomes at a glance
    • Linder S., Kopp P. Podosomes at a glance. J.Cell Sci. 2005, 118:2079-2082.
    • (2005) J.Cell Sci. , vol.118 , pp. 2079-2082
    • Linder, S.1    Kopp, P.2
  • 30
    • 38949091719 scopus 로고    scopus 로고
    • Grab, stick, pull and digest: the functional diversity of actin-associated matrix-adhesion structures. Workshop on Invadopodia, Podosomes and Focal Adhesions in Tissue Invasion
    • Machesky L., Jurdic P., Hinz B. Grab, stick, pull and digest: the functional diversity of actin-associated matrix-adhesion structures. Workshop on Invadopodia, Podosomes and Focal Adhesions in Tissue Invasion. EMBO Rep. 2008, 9:139-143.
    • (2008) EMBO Rep. , vol.9 , pp. 139-143
    • Machesky, L.1    Jurdic, P.2    Hinz, B.3
  • 32
    • 0036222549 scopus 로고    scopus 로고
    • Sensing the environment: a historical perspective on integrin signal transduction
    • Miranti C.K., Brugge J.S. Sensing the environment: a historical perspective on integrin signal transduction. Nat. Cell Biol. 2002, 4:E83-E90.
    • (2002) Nat. Cell Biol. , vol.4
    • Miranti, C.K.1    Brugge, J.S.2
  • 34
    • 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
  • 35
    • 27944442353 scopus 로고    scopus 로고
    • Altered TCR signaling from geometrically repatterned immunological synapses
    • Mossman K.D., Campi G., Groves J.T., Dustin M.L. Altered TCR signaling from geometrically repatterned immunological synapses. Science 2005, 310:1191-1193.
    • (2005) Science , vol.310 , pp. 1191-1193
    • Mossman, K.D.1    Campi, G.2    Groves, J.T.3    Dustin, M.L.4
  • 36
    • 79959541003 scopus 로고    scopus 로고
    • The 'ins' and 'outs' of podosomes and invadopodia: characteristics, formation and function
    • Murphy D.A., Courtneidge S.A. The 'ins' and 'outs' of podosomes and invadopodia: characteristics, formation and function. Nat. Rev. Mol. Cell Biol. 2011, 12:413-426.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 413-426
    • Murphy, D.A.1    Courtneidge, S.A.2
  • 37
    • 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. 1988, 7:4093-4099.
    • (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
  • 39
    • 47549105130 scopus 로고    scopus 로고
    • Sequential signals toward podosome formation in NIH-src cells
    • Oikawa T., Itoh T., Takenawa T. Sequential signals toward podosome formation in NIH-src cells. J.Cell Biol. 2008, 182:157-169.
    • (2008) J.Cell Biol. , vol.182 , pp. 157-169
    • Oikawa, T.1    Itoh, T.2    Takenawa, T.3
  • 40
    • 36849036806 scopus 로고    scopus 로고
    • Regulation of actomyosin contractility by PI3K in sensory axons
    • Orlova I., Silver L., Gallo G. Regulation of actomyosin contractility by PI3K in sensory axons. Dev. Neurobiol. 2007, 67:1843-1851.
    • (2007) Dev. Neurobiol. , vol.67 , pp. 1843-1851
    • Orlova, I.1    Silver, L.2    Gallo, G.3
  • 42
    • 33646197411 scopus 로고    scopus 로고
    • Spatiotemporal dynamics of RhoA activity in migrating cells
    • Pertz O., Hodgson L., Klemke R.L., Hahn K.M. Spatiotemporal dynamics of RhoA activity in migrating cells. Nature 2006, 440:1069-1072.
    • (2006) Nature , vol.440 , pp. 1069-1072
    • Pertz, O.1    Hodgson, L.2    Klemke, R.L.3    Hahn, K.M.4
  • 43
    • 70350417461 scopus 로고    scopus 로고
    • Matrix invasion by tumour cells: a focus on MT1-MMP trafficking to invadopodia
    • Poincloux R., Lizárraga F., Chavrier P. Matrix invasion by tumour cells: a focus on MT1-MMP trafficking to invadopodia. J.Cell Sci. 2009, 122:3015-3024.
    • (2009) J.Cell Sci. , vol.122 , pp. 3015-3024
    • Poincloux, R.1    Lizárraga, F.2    Chavrier, P.3
  • 44
    • 69549114949 scopus 로고    scopus 로고
    • WASP and SCAR/WAVE proteins: the drivers of actin assembly
    • Pollitt A.Y., Insall R.H. WASP and SCAR/WAVE proteins: the drivers of actin assembly. J.Cell Sci. 2009, 122:2575-2578.
    • (2009) J.Cell Sci. , vol.122 , pp. 2575-2578
    • Pollitt, A.Y.1    Insall, R.H.2
  • 45
    • 78649872743 scopus 로고    scopus 로고
    • Both lipid- and protein-phosphatase activities of PTEN contribute to the p53-PTEN anti-invasion pathway
    • Poon J.S., Eves R., Mak A.S. Both lipid- and protein-phosphatase activities of PTEN contribute to the p53-PTEN anti-invasion pathway. Cell Cycle 2010, 9:4450-4454.
    • (2010) Cell Cycle , vol.9 , pp. 4450-4454
    • Poon, J.S.1    Eves, R.2    Mak, A.S.3
  • 47
  • 49
    • 77949412667 scopus 로고    scopus 로고
    • Restriction of receptor movement alters cellular response: physical force sensing by EphA2
    • Salaita K., Nair P.M., Petit R.S., Neve R.M., Das D., Gray J.W., Groves J.T. Restriction of receptor movement alters cellular response: physical force sensing by EphA2. Science 2010, 327:1380-1385.
    • (2010) Science , vol.327 , pp. 1380-1385
    • Salaita, K.1    Nair, P.M.2    Petit, R.S.3    Neve, R.M.4    Das, D.5    Gray, J.W.6    Groves, J.T.7
  • 50
    • 46249118014 scopus 로고    scopus 로고
    • ERK5 promotes Src-induced podosome formation by limiting Rho activation
    • Schramp M., Ying O., Kim T.Y., Martin G.S. ERK5 promotes Src-induced podosome formation by limiting Rho activation. J.Cell Biol. 2008, 181:1195-1210.
    • (2008) J.Cell Biol. , vol.181 , pp. 1195-1210
    • Schramp, M.1    Ying, O.2    Kim, T.Y.3    Martin, G.S.4
  • 52
    • 0033587069 scopus 로고    scopus 로고
    • Receptor protein tyrosine phosphatase alpha activates Src-family kinases and controls integrin-mediated responses in fibroblasts
    • Su J., Muranjan M., Sap J. Receptor protein tyrosine phosphatase alpha activates Src-family kinases and controls integrin-mediated responses in fibroblasts. Curr. Biol. 1999, 9:505-511.
    • (1999) Curr. Biol. , vol.9 , pp. 505-511
    • Su, J.1    Muranjan, M.2    Sap, J.3
  • 54
    • 0022357441 scopus 로고
    • Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes
    • Tarone G., Cirillo D., Giancotti F.G., Comoglio P.M., Marchisio P.C. Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes. Exp. Cell Res. 1985, 159:141-157.
    • (1985) Exp. Cell Res. , vol.159 , pp. 141-157
    • Tarone, G.1    Cirillo, D.2    Giancotti, F.G.3    Comoglio, P.M.4    Marchisio, P.C.5
  • 55
    • 33846969965 scopus 로고    scopus 로고
    • Current knowledge of the large RhoGAP family of proteins
    • Tcherkezian J., Lamarche-Vane N. Current knowledge of the large RhoGAP family of proteins. Biol. Cell 2007, 99:67-86.
    • (2007) Biol. Cell , vol.99 , pp. 67-86
    • Tcherkezian, J.1    Lamarche-Vane, N.2
  • 56
    • 43149091187 scopus 로고    scopus 로고
    • PGE2-mediated podosome loss in dendritic cells is dependent on actomyosin contraction downstream of the RhoA-Rho-kinase axis
    • van Helden S.F., Oud M.M., Joosten B., Peterse N., Figdor C.G., van Leeuwen F.N. PGE2-mediated podosome loss in dendritic cells is dependent on actomyosin contraction downstream of the RhoA-Rho-kinase axis. J.Cell Sci. 2008, 121:1096-1106.
    • (2008) J.Cell Sci. , vol.121 , pp. 1096-1106
    • van Helden, S.F.1    Oud, M.M.2    Joosten, B.3    Peterse, N.4    Figdor, C.G.5    van Leeuwen, F.N.6
  • 58
    • 33645773666 scopus 로고    scopus 로고
    • Local force and geometry sensing regulate cell functions
    • Vogel V., Sheetz M. Local force and geometry sensing regulate cell functions. Nat. Rev. Mol. Cell Biol. 2006, 7:265-275.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 265-275
    • Vogel, V.1    Sheetz, M.2
  • 59
    • 60749130274 scopus 로고    scopus 로고
    • Cell fate regulation by coupling mechanical cycles to biochemical signaling pathways
    • Vogel V., Sheetz M.P. Cell fate regulation by coupling mechanical cycles to biochemical signaling pathways. Curr. Opin. Cell Biol. 2009, 21:38-46.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 38-46
    • Vogel, V.1    Sheetz, M.P.2
  • 60
    • 84857686971 scopus 로고    scopus 로고
    • Structure and function of focal adhesions
    • Wehrle-Haller B. Structure and function of focal adhesions. Curr. Opin. Cell Biol. 2012, 24:116-124.
    • (2012) Curr. Opin. Cell Biol. , vol.24 , pp. 116-124
    • Wehrle-Haller, B.1
  • 61
    • 22944438407 scopus 로고    scopus 로고
    • FAK-mediated src phosphorylation of endophilin A2 inhibits endocytosis of MT1-MMP and promotes ECM degradation
    • Wu X., Gan B., Yoo Y., Guan J.L. FAK-mediated src phosphorylation of endophilin A2 inhibits endocytosis of MT1-MMP and promotes ECM degradation. Dev. Cell 2005, 9:185-196.
    • (2005) Dev. Cell , vol.9 , pp. 185-196
    • Wu, X.1    Gan, B.2    Yoo, Y.3    Guan, J.L.4
  • 62
    • 0038576209 scopus 로고    scopus 로고
    • Kinetic analysis of receptor-activated phosphoinositide turnover
    • Xu C., Watras J., Loew L.M. Kinetic analysis of receptor-activated phosphoinositide turnover. J.Cell Biol. 2003, 161:779-791.
    • (2003) J.Cell Biol. , vol.161 , pp. 779-791
    • Xu, C.1    Watras, J.2    Loew, L.M.3
  • 63
    • 77957767638 scopus 로고    scopus 로고
    • Engineering supported membranes for cell biology
    • Yu C.H., Groves J.T. Engineering supported membranes for cell biology. Med. Biol. Eng. Comput. 2010, 48:955-963.
    • (2010) Med. Biol. Eng. Comput. , vol.48 , pp. 955-963
    • Yu, C.H.1    Groves, J.T.2
  • 64
    • 77955623486 scopus 로고    scopus 로고
    • Altered actin centripetal retrograde flow in physically restricted immunological synapses
    • Yu C.H., Wu H.J., Kaizuka Y., Vale R.D., Groves J.T. Altered actin centripetal retrograde flow in physically restricted immunological synapses. PLoS ONE 2010, 5:e11878.
    • (2010) PLoS ONE , vol.5
    • Yu, C.H.1    Wu, H.J.2    Kaizuka, Y.3    Vale, R.D.4    Groves, J.T.5
  • 65
    • 84855500059 scopus 로고    scopus 로고
    • Early integrin binding to Arg-Gly-Asp peptide activates actin polymerization and contractile movement that stimulates outward translocation
    • Yu C.H., Law J.B., Suryana M., Low H.Y., Sheetz M.P. Early integrin binding to Arg-Gly-Asp peptide activates actin polymerization and contractile movement that stimulates outward translocation. Proc. Natl. Acad. Sci. USA 2011, 108:20585-20590.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 20585-20590
    • Yu, C.H.1    Law, J.B.2    Suryana, M.3    Low, H.Y.4    Sheetz, M.P.5
  • 66
    • 84864920732 scopus 로고    scopus 로고
    • Spatial-temporal reorganization of activated integrins
    • Yu C.H., Luo W., Sheetz M.P. Spatial-temporal reorganization of activated integrins. Cell Adhes. Migr. 2012, 6:280-284.
    • (2012) Cell Adhes. Migr. , vol.6 , pp. 280-284
    • Yu, C.H.1    Luo, W.2    Sheetz, M.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.