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Volumn 5, Issue , 2014, Pages

Regulation of focal adhesion formation by a vinculin-Arp2/3 hybrid complex

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN RELATED PROTEIN 2; ACTIN RELATED PROTEIN 3; ALPHA ACTININ; P41 ARC PROTEIN; PROTEIN; UNCLASSIFIED DRUG; VINCULIN; ACTIN RELATED PROTEIN 2-3 COMPLEX; ACTININ; FLUORESCEIN ISOTHIOCYANATE; SMALL INTERFERING RNA;

EID: 84899885606     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms4758     Document Type: Article
Times cited : (81)

References (55)
  • 1
    • 0016489782 scopus 로고
    • Adhesions of fibroblasts to substratum during contact inhibition observed by interference reflection microscopy
    • Abercrombie, M. & Dunn, G. A. Adhesions of fibroblasts to substratum during contact inhibition observed by interference reflection microscopy. Exp. Cell Res. 92, 57-62 (1975).
    • (1975) Exp. Cell Res. , vol.92 , pp. 57-62
    • Abercrombie, M.1    Dunn, G.A.2
  • 2
    • 0015104295 scopus 로고
    • The locomotion of fibroblasts in culture. IV. Electron microscopy of the leading lamella
    • Abercrombie, M., Heaysman, J. E. & Pegrum, S. M. The locomotion of fibroblasts in culture. IV. Electron microscopy of the leading lamella. Exp. Cell Res. 67, 359-367 (1971).
    • (1971) Exp. Cell Res. , vol.67 , pp. 359-367
    • Abercrombie, M.1    Heaysman, J.E.2    Pegrum, S.M.3
  • 3
    • 0017143820 scopus 로고
    • Cell-to-substrate contacts in living fibroblasts: An interference reflexion study with an evaluation of the technique
    • Izzard, C. S. & Lochner, L. R. Cell-to-substrate contacts in living fibroblasts: an interference reflexion study with an evaluation of the technique. J. Cell Sci. 21, 129-159 (1976).
    • (1976) J. Cell Sci. , vol.21 , pp. 129-159
    • Izzard, C.S.1    Lochner, L.R.2
  • 4
    • 0019230475 scopus 로고
    • Formation of cell-to-substrate contacts during fibroblast motility: An interference-reflexion study
    • Izzard, C. S. & Lochner, L. R. Formation of cell-to-substrate contacts during fibroblast motility: an interference-reflexion study. J. Cell Sci. 42, 81-116 (1980).
    • (1980) J. Cell Sci. , vol.42 , pp. 81-116
    • Izzard, C.S.1    Lochner, L.R.2
  • 6
    • 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 24, 447-458 (2013).
    • (2013) Dev. Cell , vol.24 , pp. 447-458
    • Wolfenson, H.1    Lavelin, I.2    Geiger, B.3
  • 7
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R. O. Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69, 11-25 (1992).
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 9
    • 70350418724 scopus 로고    scopus 로고
    • Actin machinery and mechanosensitivity in invadopodia, podosomes and focal adhesions
    • Albiges-Rizo, C., Destaing, O., Fourcade, B., Planus, E. & Block, M. R. Actin machinery and mechanosensitivity in invadopodia, podosomes and focal adhesions. J. Cell Sci. 122, 3037-3049 (2009).
    • (2009) J. Cell Sci. , vol.122 , pp. 3037-3049
    • Albiges-Rizo, C.1    Destaing, O.2    Fourcade, B.3    Planus, E.4    Block, M.R.5
  • 11
    • 0034755942 scopus 로고    scopus 로고
    • Molecular complexity and dynamics of cell-matrix adhesions
    • Zamir, E. & Geiger, B. Molecular complexity and dynamics of cell-matrix adhesions. J. Cell Sci. 114, 3583-3590 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 3583-3590
    • Zamir, E.1    Geiger, B.2
  • 13
    • 77956064817 scopus 로고    scopus 로고
    • Cell adhesion: Integrating cytoskeletal dynamics and cellular tension
    • Parsons, J. T., Horwitz, A. R. & Schwartz, M. A. Cell adhesion: integrating cytoskeletal dynamics and cellular tension. Nat. Rev. Mol. Cell Biol. 11, 633-643 (2010).
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 633-643
    • Parsons, J.T.1    Horwitz, A.R.2    Schwartz, M.A.3
  • 14
    • 84857686971 scopus 로고    scopus 로고
    • Structure and function of focal adhesions
    • Wehrle-Haller, B. Structure and function of focal adhesions. Curr. Opin. Cell Biol. 24, 116-124 (2012).
    • (2012) Curr. Opin. Cell Biol. , vol.24 , pp. 116-124
    • Wehrle-Haller, B.1
  • 15
    • 77951737987 scopus 로고    scopus 로고
    • The switchable integrin adhesome
    • Zaidel-Bar, R. & Geiger, B. The switchable integrin adhesome. J. Cell Sci. 123, 1385-1388 (2010).
    • (2010) J. Cell Sci. , vol.123 , pp. 1385-1388
    • Zaidel-Bar, R.1    Geiger, B.2
  • 16
    • 77956412906 scopus 로고    scopus 로고
    • Dissecting the molecular architecture of integrin adhesion sites by cryo-electron tomography
    • Patla, I. et al. Dissecting the molecular architecture of integrin adhesion sites by cryo-electron tomography. Nat. Cell Biol. 12, 909-915 (2010).
    • (2010) Nat. Cell Biol. , vol.12 , pp. 909-915
    • Patla, I.1
  • 17
    • 78649483796 scopus 로고    scopus 로고
    • Nanoscale architecture of integrin-based cell adhesions
    • Kanchanawong, P. et al. Nanoscale architecture of integrin-based cell adhesions. Nature 468, 580-584 (2010).
    • (2010) Nature , vol.468 , pp. 580-584
    • Kanchanawong, P.1
  • 18
    • 77951153298 scopus 로고    scopus 로고
    • Proteomic analysis of integrin-associated complexes identifies RCC2 as a dual regulator of rac1 and arf6
    • Humphries, J. D. et al. Proteomic analysis of integrin-associated complexes identifies RCC2 as a dual regulator of Rac1 and Arf6. Sci. Signal. 2, ra51 (2009).
    • (2009) Sci. Signal. , vol.2
    • Humphries, J.D.1
  • 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. 12, 259-266 (2011).
    • (2011) EMBO Rep. , vol.12 , pp. 259-266
    • Schiller, H.B.1    Friedel, C.C.2    Boulegue, C.3    Fassler, R.4
  • 20
    • 79953303384 scopus 로고    scopus 로고
    • Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for beta-pix in negative regulation of focal adhesion maturation
    • Kuo, J. C., Han, X., Hsiao, C. T., Yates, 3rd J. R. & Waterman, C. M. Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for beta-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13, 383-393 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 383-393
    • Kuo, J.C.1    Han, X.2    Hsiao, C.T.3    Yates III, J.R.4    Waterman, C.M.5
  • 21
    • 0034725593 scopus 로고    scopus 로고
    • Integrins and actin filaments: Reciprocal regulation of cell adhesion and signaling
    • Calderwood, D. A., Shattil, S. J. & Ginsberg, M. H. Integrins and actin filaments: reciprocal regulation of cell adhesion and signaling. J. Biol. Chem. 275, 22607-22610 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 22607-22610
    • Calderwood, D.A.1    Shattil, S.J.2    Ginsberg, M.H.3
  • 22
    • 0034906978 scopus 로고    scopus 로고
    • ActA and human zyxin harbour arp2/3-independent actinpolymerization activity
    • Fradelizi, J. et al. ActA and human zyxin harbour Arp2/3-independent actinpolymerization activity. Nat. Cell Biol. 3, 699-707 (2001).
    • (2001) Nat. Cell Biol. , vol.3 , pp. 699-707
    • Fradelizi, J.1
  • 23
    • 3042835147 scopus 로고    scopus 로고
    • Integrating an integrin: A direct route to actin
    • Blystone, S. D. Integrating an integrin: a direct route to actin. Biochim. Biophys. Acta. 1692, 47-54 (2004).
    • (2004) Biochim. Biophys. Acta. , vol.1692 , pp. 47-54
    • Blystone, S.D.1
  • 24
    • 0031967863 scopus 로고    scopus 로고
    • Sites of monomeric actin incorporation in living PtK2 and REF-52 cells
    • Turnacioglu, K. K., Sanger, J. W. & Sanger, J. M. Sites of monomeric actin incorporation in living PtK2 and REF-52 cells. Cell. Motil. Cytoskeleton 40, 59-70 (1998).
    • (1998) Cell. Motil. Cytoskeleton , vol.40 , pp. 59-70
    • Turnacioglu, K.K.1    Sanger, J.W.2    Sanger, J.M.3
  • 25
    • 0020610627 scopus 로고
    • Subcellular distribution of rhodamine-actin microinjected into living fibroblastic cells
    • Glacy, S. D. Subcellular distribution of rhodamine-actin microinjected into living fibroblastic cells. J. Cell Biol. 97, 1207-1213 (1983).
    • (1983) J. Cell Biol. , vol.97 , pp. 1207-1213
    • Glacy, S.D.1
  • 26
    • 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. et al. 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. 153, 1175-1186 (2001).
    • (2001) J. Cell Biol. , vol.153 , pp. 1175-1186
    • Riveline, D.1
  • 28
    • 84977668746 scopus 로고    scopus 로고
    • Myosin 1E localizes to actin polymerization sites in lamellipodia, affecting actin dynamics and adhesion formation
    • Gupta, P. et al. Myosin 1E localizes to actin polymerization sites in lamellipodia, affecting actin dynamics and adhesion formation. Biol. Open 2, 1288-1299 (2013).
    • (2013) Biol. Open , vol.2 , pp. 1288-1299
    • Gupta, P.1
  • 29
    • 35648943165 scopus 로고    scopus 로고
    • MDia2 regulates actin and focal adhesion dynamics and organization in the lamella for efficient epithelial cell migration
    • Gupton, S. L., Eisenmann, K., Alberts, A. S. & Waterman-Storer, C. M. mDia2 regulates actin and focal adhesion dynamics and organization in the lamella for efficient epithelial cell migration. J. Cell Sci. 120, 3475-3487 (2007).
    • (2007) J. Cell Sci. , vol.120 , pp. 3475-3487
    • Gupton, S.L.1    Eisenmann, K.2    Alberts, A.S.3    Waterman-Storer, C.M.4
  • 30
    • 49449117636 scopus 로고    scopus 로고
    • Formin 1-isoform IV deficient cells exhibit defects in cell spreading and focal adhesion formation
    • Dettenhofer, M., Zhou, F. & Leder, P. Formin 1-isoform IV deficient cells exhibit defects in cell spreading and focal adhesion formation. PLoS ONE 3, e2497 (2008).
    • (2008) PLoS ONE , vol.3
    • Dettenhofer, M.1    Zhou, F.2    Leder, P.3
  • 31
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
    • Svitkina, T. M. & Borisy, G. G. Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol. 145, 1009-1026 (1999).
    • (1999) J. Cell Biol. , vol.145 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 32
    • 0036909561 scopus 로고    scopus 로고
    • Structure and function of the arp2/3 complex
    • Pollard, T. D. & Beltzner, C. C. Structure and function of the Arp2/3 complex. Curr. Opin. Struct. Biol. 12, 768-774 (2002).
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 768-774
    • Pollard, T.D.1    Beltzner, C.C.2
  • 33
    • 38049078282 scopus 로고    scopus 로고
    • The structural basis of actin filament branching by the arp2/3 complex
    • Rouiller, I. et al. The structural basis of actin filament branching by the Arp2/3 complex. J. Cell Biol. 180, 887-895 (2008).
    • (2008) J. Cell Biol. , vol.180 , pp. 887-895
    • Rouiller, I.1
  • 34
    • 0035930328 scopus 로고    scopus 로고
    • Reconstitution of human arp2/3 complex reveals critical roles of individual subunits in complex structure and activity
    • Gournier, H., Goley, E. D., Niederstrasser, H., Trinh, T. & Welch, M. D. Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity. Mol. Cell 8, 1041-1052 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 1041-1052
    • Gournier, H.1    Goley, E.D.2    Niederstrasser, H.3    Trinh, T.4    Welch, M.D.5
  • 35
    • 0035941045 scopus 로고    scopus 로고
    • Crystal structure of arp2/3 complex
    • Robinson, R. C. et al. Crystal structure of Arp2/3 complex. Science 294, 1679-1684 (2001).
    • (2001) Science , vol.294 , pp. 1679-1684
    • Robinson, R.C.1
  • 36
    • 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
  • 37
    • 0742289599 scopus 로고    scopus 로고
    • Identification of functionally important residues of arp2/3 complex by analysis of homology models from diverse species
    • Beltzner, C. C. & Pollard, T. D. Identification of functionally important residues of Arp2/3 complex by analysis of homology models from diverse species. J. Mol. Biol. 336, 551-565 (2004).
    • (2004) J. Mol. Biol. , vol.336 , pp. 551-565
    • Beltzner, C.C.1    Pollard, T.D.2
  • 38
    • 0037049555 scopus 로고    scopus 로고
    • Recruitment of the arp2/3 complex to vinculin: Coupling membrane protrusion to matrix adhesion
    • DeMali, K. A., Barlow, C. A. & Burridge, K. Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion. J. Cell Biol. 159, 881-891 (2002).
    • (2002) J. Cell Biol. , vol.159 , pp. 881-891
    • Demali, K.A.1    Barlow, C.A.2    Burridge, K.3
  • 39
    • 34548316989 scopus 로고    scopus 로고
    • Focal adhesion kinase controls actin assembly via a FERMmediated interaction with the arp2/3 complex
    • Serrels, B. et al. Focal adhesion kinase controls actin assembly via a FERMmediated interaction with the Arp2/3 complex. Nat. Cell Biol. 9, 1046-1056 (2007).
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1046-1056
    • Serrels, B.1
  • 40
    • 0018692430 scopus 로고
    • A 130 K protein from chicken gizzard: Its localization at the termini of microfilament bundles in cultured chicken cells
    • Geiger, B. A 130 K protein from chicken gizzard: its localization at the termini of microfilament bundles in cultured chicken cells. Cell 18, 193-205 (1979).
    • (1979) Cell , vol.18 , pp. 193-205
    • Geiger, B.1
  • 41
    • 0019320755 scopus 로고
    • A rapid purification of alpha-actinin, filamin, and a 130,000-dalton protein from smooth muscle
    • Feramisco, J. R. & Burridge, K. A rapid purification of alpha-actinin, filamin, and a 130,000-dalton protein from smooth muscle. J. Biol. Chem. 255, 1194-1199 (1980).
    • (1980) J. Biol. Chem. , vol.255 , pp. 1194-1199
    • Feramisco, J.R.1    Burridge, K.2
  • 42
    • 0025008074 scopus 로고
    • Paxillin: A new vinculin-binding protein present in focal adhesions
    • Turner, C. E., Glenney, Jr. J. R. & Burridge, K. Paxillin: a new vinculin-binding protein present in focal adhesions. J. Cell Biol. 111, 1059-1068 (1990).
    • (1990) J. Cell Biol. , vol.111 , pp. 1059-1068
    • Turner, C.E.1    Glenney Jr., J.R.2    Burridge, K.3
  • 43
    • 0019321171 scopus 로고
    • New, rapid methods for purifying alpha-actinin from chicken gizzard and chicken pectoral muscle
    • Langer, B. G. & Pepe, F. A. New, rapid methods for purifying alpha-actinin from chicken gizzard and chicken pectoral muscle. J. Biol. Chem. 255, 5429-5434 (1980).
    • (1980) J. Biol. Chem. , vol.255 , pp. 5429-5434
    • Langer, B.G.1    Pepe, F.A.2
  • 44
    • 0020805412 scopus 로고
    • A new protein of adhesion plaques and ruffling membranes
    • Burridge, K. & Connell, L. A new protein of adhesion plaques and ruffling membranes. J. Cell Biol. 97, 359-367 (1983).
    • (1983) J. Cell Biol. , vol.97 , pp. 359-367
    • Burridge, K.1    Connell, L.2
  • 45
    • 84884485442 scopus 로고    scopus 로고
    • Exposing the subunit diversity within protein complexes: A mass spectrometry approach
    • Rozen, S. et al. Exposing the subunit diversity within protein complexes: A mass spectrometry approach. Methods 59, 270-277 (2013).
    • (2013) Methods , vol.59 , pp. 270-277
    • Rozen, S.1
  • 46
    • 77950339600 scopus 로고    scopus 로고
    • How far can we go with structural mass spectrometry of protein complexes?
    • Sharon, M. How far can we go with structural mass spectrometry of protein complexes? J. Am. Soc. Mass. Spectrom. 21, 487-500 (2010).
    • (2010) J. Am. Soc. Mass. Spectrom. , vol.21 , pp. 487-500
    • Sharon, M.1
  • 47
    • 44649150563 scopus 로고    scopus 로고
    • Subunit architecture of intact protein complexes from mass spectrometry and homology modeling
    • Taverner, T. et al. Subunit architecture of intact protein complexes from mass spectrometry and homology modeling. Acc. Chem. Res. 41, 617-627 (2008).
    • (2008) Acc. Chem. Res. , vol.41 , pp. 617-627
    • Taverner, T.1
  • 48
    • 34548426979 scopus 로고    scopus 로고
    • The role of mass spectrometry in structure elucidation of dynamic protein complexes
    • Sharon, M. & Robinson, C. V. The role of mass spectrometry in structure elucidation of dynamic protein complexes. Annu. Rev. Biochem. 76, 167-193 (2007).
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 167-193
    • Sharon, M.1    Robinson, C.V.2
  • 49
    • 0031051993 scopus 로고    scopus 로고
    • Structure, subunit topology, and actin-binding activity of the arp2/3 complex from acanthamoeba
    • Mullins, R. D., Stafford, W. F. & Pollard, T. D. Structure, subunit topology, and actin-binding activity of the Arp2/3 complex from Acanthamoeba. J. Cell Biol. 136, 331-343 (1997).
    • (1997) J. Cell Biol. , vol.136 , pp. 331-343
    • Mullins, R.D.1    Stafford, W.F.2    Pollard, T.D.3
  • 50
    • 33846827258 scopus 로고    scopus 로고
    • Visualizing arp2/3 complex activation mediated by binding of ATP and WASp using structural mass spectrometry
    • Kiselar, J. G., Mahaffy, R., Pollard, T. D., Almo, S. C. & Chance, M. R. Visualizing Arp2/3 complex activation mediated by binding of ATP and WASp using structural mass spectrometry. Proc. Natl Acad. Sci. USA 104, 1552-1557 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 1552-1557
    • Kiselar, J.G.1    Mahaffy, R.2    Pollard, T.D.3    Almo, S.C.4    Chance, M.R.5
  • 51
    • 42949099523 scopus 로고    scopus 로고
    • X-ray scattering study of activated arp2/3 complex with bound actin-WCA
    • Boczkowska, M. et al. X-ray scattering study of activated Arp2/3 complex with bound actin-WCA. Structure. 16, 695-704 (2008).
    • (2008) Structure. , vol.16 , pp. 695-704
    • Boczkowska, M.1
  • 52
    • 77950874245 scopus 로고    scopus 로고
    • The p40/ARPC1 subunit of arp2/3 complex performs multiple essential roles in WASp-regulated actin nucleation
    • Balcer, H. I., Daugherty-Clarke, K. & Goode, B. L. The p40/ARPC1 subunit of Arp2/3 complex performs multiple essential roles in WASp-regulated actin nucleation. J. Biol. Chem. 285, 8481-8491 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 8481-8491
    • Balcer, H.I.1    Daugherty-Clarke, K.2    Goode, B.L.3
  • 53
    • 0026694947 scopus 로고
    • In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis
    • Rosenfeld, J., Capdevielle, J., Guillemot, J. C. & Ferrara, P. In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis. Anal. Biochem. 203, 173-179 (1992).
    • (1992) Anal. Biochem. , vol.203 , pp. 173-179
    • Rosenfeld, J.1    Capdevielle, J.2    Guillemot, J.C.3    Ferrara, P.4
  • 54
    • 1542723081 scopus 로고    scopus 로고
    • Collisional cooling of large ions in electrospray mass spectrometry
    • Chernushevich, I. V. & Thomson, B. A. Collisional cooling of large ions in electrospray mass spectrometry. Anal. Chem. 76, 1754-1760 (2004).
    • (2004) Anal. Chem. , vol.76 , pp. 1754-1760
    • Chernushevich, I.V.1    Thomson, B.A.2
  • 55
    • 80355140625 scopus 로고    scopus 로고
    • Analyzing large protein complexes by structural mass spectrometry
    • Kirshenbaum, N., Michaelevski, I. & Sharon, M. Analyzing large protein complexes by structural mass spectrometry. J. Vis. Exp. 40, 1954 (2010).
    • (2010) J. Vis. Exp. , vol.40 , pp. 1954
    • Kirshenbaum, N.1    Michaelevski, I.2    Sharon, M.3


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