메뉴 건너뛰기




Volumn 174, Issue 3, 2006, Pages 447-458

Supervillin modulation of focal adhesions involving TRIP6/ZRP-1

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; FAS ANTIGEN; FIBRONECTIN; LIM PROTEIN; MEMBRANE PROTEIN; MYOSIN II; PROTEIN SUPERVILLIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR TRIP6; UNCLASSIFIED DRUG; ZYXIN;

EID: 33746595301     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200512051     Document Type: Article
Times cited : (51)

References (50)
  • 1
    • 0036377106 scopus 로고    scopus 로고
    • Biological aspects of signal transduction by cell adhesion receptors
    • Alahari, S.K., P.J. Reddig, and R.L. Juliano. 2002. Biological aspects of signal transduction by cell adhesion receptors. Int. Rev. Cytol. 220:145-184.
    • (2002) Int. Rev. Cytol. , vol.220 , pp. 145-184
    • Alahari, S.K.1    Reddig, P.J.2    Juliano, R.L.3
  • 2
    • 0035945353 scopus 로고    scopus 로고
    • Marching at the front and dragging behind: Differential αVβ3-integrin turnover regulates focal adhesion behavior
    • Ballestrem, C., B. Hinz, B.A. Imhof, and B. Wehrle-Haller. 2001. Marching at the front and dragging behind: differential αVβ3-integrin turnover regulates focal adhesion behavior. J. Cell Biol. 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
  • 3
    • 0035858878 scopus 로고    scopus 로고
    • Nascent focal adhesions are responsible for the generation of strong propulsive forces in migrating fibroblasts
    • Beningo, K.A., M. Dembo, I. Kaverina, J.V. Small, and Y.L. Wang. 2001. Nascent focal adhesions are responsible for the generation of strong propulsive forces in migrating fibroblasts. J. Cell Biol. 153:881-888.
    • (2001) J. Cell Biol. , vol.153 , pp. 881-888
    • Beningo, K.A.1    Dembo, M.2    Kaverina, I.3    Small, J.V.4    Wang, Y.L.5
  • 4
    • 2342472716 scopus 로고    scopus 로고
    • Focal adhesion and actin dynamics: A place where kinases and proteases meet to promote invasion
    • Carragher, N.O., and M.C. Frame. 2004. Focal adhesion and actin dynamics: a place where kinases and proteases meet to promote invasion. Trends Cell Biol. 14:241-249.
    • (2004) Trends Cell Biol. , vol.14 , pp. 241-249
    • Carragher, N.O.1    Frame, M.C.2
  • 6
    • 3042589327 scopus 로고    scopus 로고
    • Endoglin controls cell migration and composition of focal adhesions: Function of the cytosolic domain
    • Conley, B.A., R. Koleva, J.D. Smith, D. Kacer, D. Zhang, C. Bernabeu, and C.P. Vary. 2004. Endoglin controls cell migration and composition of focal adhesions: function of the cytosolic domain. J. Biol. Chem. 279:27440-27449.
    • (2004) J. Biol. Chem. , vol.279 , pp. 27440-27449
    • Conley, B.A.1    Koleva, R.2    Smith, J.D.3    Kacer, D.4    Zhang, D.5    Bernabeu, C.6    Vary, C.P.7
  • 7
    • 0034010331 scopus 로고    scopus 로고
    • The zyxin-related protein TRIP6 interacts with PDZ motifs in the adaptor protein RIL and the protein tyrosine phosphatase PTP-BL
    • Cuppen, E., M. van Ham, D.G. Wansink, A. de Leeuw, B. Wieringa, and W. Hendriks. 2000. The zyxin-related protein TRIP6 interacts with PDZ motifs in the adaptor protein RIL and the protein tyrosine phosphatase PTP-BL. Eur. J. Cell Biol. 79:283-293.
    • (2000) Eur. J. Cell Biol. , vol.79 , pp. 283-293
    • Cuppen, E.1    Van Ham, M.2    Wansink, D.G.3    De Leeuw, A.4    Wieringa, B.5    Hendriks, W.6
  • 9
    • 0037175402 scopus 로고    scopus 로고
    • The relationship between force and focal complex development
    • Galbraith, C.G., K.M. Yamada, and M.P. Sheetz. 2002. The relationship between force and focal complex development. J. Cell Biol. 159:695-705.
    • (2002) J. Cell Biol. , vol.159 , pp. 695-705
    • Galbraith, C.G.1    Yamada, K.M.2    Sheetz, M.P.3
  • 11
    • 0030828053 scopus 로고    scopus 로고
    • Structural and functional similarities between the human cytoskeletal protein zyxin and the ActA protein of Listeria monocytogenes
    • Golsteyn, R.M., M.C. Beckerle, T. Koay, and E. Friederich. 1997. Structural and functional similarities between the human cytoskeletal protein zyxin and the ActA protein of Listeria monocytogenes. J. Cell Sci. 110:1893-1906.
    • (1997) J. Cell Sci. , vol.110 , pp. 1893-1906
    • Golsteyn, R.M.1    Beckerle, M.C.2    Koay, T.3    Friederich, E.4
  • 12
    • 27744534555 scopus 로고    scopus 로고
    • Down-regulation of TRIP6 gene expression induces actin cytoskeleton rearrangements in human carcinoma cell lines
    • Guryanova, O.A., A.A. Sablina, P.M. Chumakov, and E.I. Frolova. 2005. Down-regulation of TRIP6 gene expression induces actin cytoskeleton rearrangements in human carcinoma cell lines. Mol. Biol. 39:792-795.
    • (2005) Mol. Biol. , vol.39 , pp. 792-795
    • Guryanova, O.A.1    Sablina, A.A.2    Chumakov, P.M.3    Frolova, E.I.4
  • 13
    • 0034740693 scopus 로고    scopus 로고
    • Mechanism and role of PDZ domains in signaling complex assembly
    • Harris, B.Z., and W.A. Lim. 2001. Mechanism and role of PDZ domains in signaling complex assembly. J. Cell Sci. 114:3219-3231.
    • (2001) J. Cell Sci. , vol.114 , pp. 3219-3231
    • Harris, B.Z.1    Lim, W.A.2
  • 14
    • 0035159094 scopus 로고    scopus 로고
    • Alpha-smooth muscle actin expression upregulates fibroblast contractile activity
    • Hinz, B., G. Celetta, J.J. Tomasek, G. Gabbiani, and C. Chaponnier. 2001. Alpha-smooth muscle actin expression upregulates fibroblast contractile activity. Mol. Biol. Cell. 12:2730-2741.
    • (2001) Mol. Biol. Cell. , vol.12 , pp. 2730-2741
    • Hinz, B.1    Celetta, G.2    Tomasek, J.J.3    Gabbiani, G.4    Chaponnier, C.5
  • 15
    • 33644503878 scopus 로고    scopus 로고
    • Genetic ablation of zyxin causes Mena/VASP mislocalization, increased motility, and deficits in actin remodeling
    • Hoffman, L.M., C.C. Jensen, S. Kloeker, C.L. Wang, M. Yoshigi, and M.C. Beckerle. 2006. Genetic ablation of zyxin causes Mena/VASP mislocalization, increased motility, and deficits in actin remodeling. J. Cell Biol. 172:771-782.
    • (2006) J. Cell Biol. , vol.172 , pp. 771-782
    • Hoffman, L.M.1    Jensen, C.C.2    Kloeker, S.3    Wang, C.L.4    Yoshigi, M.5    Beckerle, M.C.6
  • 18
    • 8444240109 scopus 로고    scopus 로고
    • The LIM domain: From the cytoskeleton to the nucleus
    • Kadrmas, J.L., and M.C. Beckerle. 2004. The LIM domain: from the cytoskeleton to the nucleus. Nat. Rev. Mol. Cell Biol. 5:920-931.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 920-931
    • Kadrmas, J.L.1    Beckerle, M.C.2
  • 19
    • 5444233785 scopus 로고    scopus 로고
    • A nuclear isoform of the focal adhesion LIM-domain protein Trip6 integrates activating and repressing signals at AP-1- and NF-kappaB-regulated promoters
    • Kassel, O., S. Schneider, C. Heilbock, M. Litfin, M. Gottlicher, and P. Herrlich. 2004. A nuclear isoform of the focal adhesion LIM-domain protein Trip6 integrates activating and repressing signals at AP-1- and NF-kappaB-regulated promoters. Genes Dev. 18:2518-2528.
    • (2004) Genes Dev. , vol.18 , pp. 2518-2528
    • Kassel, O.1    Schneider, S.2    Heilbock, C.3    Litfin, M.4    Gottlicher, M.5    Herrlich, P.6
  • 20
  • 22
    • 21744441622 scopus 로고    scopus 로고
    • c-Src-mediated phosphorylation of TRIP6 regulates its function in lysophosphatidic acid-induced cell migration
    • Lai, Y.J., C.S. Chen, W.C. Lin, and F.T. Lin. 2005. c-Src-mediated phosphorylation of TRIP6 regulates its function in lysophosphatidic acid-induced cell migration. Mol. Cell. Biol. 25:5859-5868.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5859-5868
    • Lai, Y.J.1    Chen, C.S.2    Lin, W.C.3    Lin, F.T.4
  • 23
    • 33644901594 scopus 로고    scopus 로고
    • Mechanical forces alter zyxin unbinding kinetics within focal adhesions of living cells
    • Lele, T.P., J. Pendse, S. Kumar, M. Salanga, J. Karavitis, and D.E. Ingber. 2006. Mechanical forces alter zyxin unbinding kinetics within focal adhesions of living cells. J. Cell. Physiol. 207:187-194.
    • (2006) J. Cell. Physiol. , vol.207 , pp. 187-194
    • Lele, T.P.1    Pendse, J.2    Kumar, S.3    Salanga, M.4    Karavitis, J.5    Ingber, D.E.6
  • 24
    • 14644412359 scopus 로고    scopus 로고
    • TRIP6 is a RIP2-associated common signaling component of multiple NF-kappaB activation pathways
    • Li, L., L.H. Bin, F. Li, Y. Liu, D. Chen, Z. Zhai, and H.B. Shu. 2005. TRIP6 is a RIP2-associated common signaling component of multiple NF-kappaB activation pathways. J. Cell Sci. 118:555-563.
    • (2005) J. Cell Sci. , vol.118 , pp. 555-563
    • Li, L.1    Bin, L.H.2    Li, F.3    Liu, Y.4    Chen, D.5    Zhai, Z.6    Shu, H.B.7
  • 25
    • 0024461009 scopus 로고
    • Cell adhesion to fibronectin and tenascin: Quantitative measurements of initial binding and subsequent strengthening response
    • Lotz, M.M., C.A. Burdsal, H.P. Erickson, and D.R. McClay. 1989. Cell adhesion to fibronectin and tenascin: quantitative measurements of initial binding and subsequent strengthening response. J. Cell Biol. 109:1795- 1805.
    • (1989) J. Cell Biol. , vol.109 , pp. 1795-1805
    • Lotz, M.M.1    Burdsal, C.A.2    Erickson, H.P.3    McClay, D.R.4
  • 26
    • 0033575252 scopus 로고    scopus 로고
    • ZRP-1, a zyxin-related protein, interacts with the second PDZ domain of the cytosolic protein tyrosine phosphatase hPTP1E
    • Murthy, K.K., K. Clark, Y. Fortin, S.H. Shen, and D. Banville. 1999. ZRP-1, a zyxin-related protein, interacts with the second PDZ domain of the cytosolic protein tyrosine phosphatase hPTP1E. J. Biol. Chem. 274:20679- 20687.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20679-20687
    • Murthy, K.K.1    Clark, K.2    Fortin, Y.3    Shen, S.H.4    Banville, D.5
  • 27
    • 0037044851 scopus 로고    scopus 로고
    • Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes
    • Nebl, T., K.N. Pestonjamasp, J.D. Leszyk, J.L. Crowley, S.W. Oh, and E.J. Luna. 2002. Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes. J. Biol. Chem. 277:43399-43409.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43399-43409
    • Nebl, T.1    Pestonjamasp, K.N.2    Leszyk, J.D.3    Crowley, J.L.4    Oh, S.W.5    Luna, E.J.6
  • 28
    • 0038348502 scopus 로고    scopus 로고
    • Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton
    • Oh, S.W., R.K. Pope, K.P. Smith, J.L. Crowley, T. Nebl, J.B. Lawrence, and E.J. Luna. 2003. Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton. J. Cell Sci. 116:2261-2275.
    • (2003) J. Cell Sci. , vol.116 , pp. 2261-2275
    • Oh, S.W.1    Pope, R.K.2    Smith, K.P.3    Crowley, J.L.4    Nebl, T.5    Lawrence, J.B.6    Luna, E.J.7
  • 29
    • 0030831613 scopus 로고    scopus 로고
    • Supervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily
    • Pestonjamasp, K.N., R.K. Pope, J.D. Wulfkuhle, and E.J. Luna. 1997. Supervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily. J. Cell Biol. 139:1255-1269.
    • (1997) J. Cell Biol. , vol.139 , pp. 1255-1269
    • Pestonjamasp, K.N.1    Pope, R.K.2    Wulfkuhle, J.D.3    Luna, E.J.4
  • 30
    • 0037462676 scopus 로고    scopus 로고
    • The focal adhesion and nuclear targeting capacity of the LIM-containing lipoma-preferred partner (LPP) protein
    • Petit, M.M., S.M. Meulemans, and W.J. Van de Ven. 2003. The focal adhesion and nuclear targeting capacity of the LIM-containing lipoma-preferred partner (LPP) protein. J. Biol. Chem. 278:2157-2168.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2157-2168
    • Petit, M.M.1    Meulemans, S.M.2    Van De Ven, W.J.3
  • 31
    • 24144501081 scopus 로고    scopus 로고
    • The tumor suppressor Scrib selectively interacts with specific members of the zyxin family of proteins
    • Petit, M.M., K.R. Crombez, H.B. Vervenne, N. Weyns, and W.J. Van de Ven. 2005. The tumor suppressor Scrib selectively interacts with specific members of the zyxin family of proteins. FEBS Lett. 579:5061-5068.
    • (2005) FEBS Lett. , vol.579 , pp. 5061-5068
    • Petit, M.M.1    Crombez, K.R.2    Vervenne, H.B.3    Weyns, N.4    Van De Ven, W.J.5
  • 35
    • 3543041235 scopus 로고    scopus 로고
    • Endoglin regulates cytoskeletal organization through binding to ZRP-1, a member of the Lim family of proteins
    • Sanz-Rodriguez, F., M. Guerrero-Esteo, L.M. Botella, D. Banville, C.P. Vary, and C. Bernabeu. 2004. Endoglin regulates cytoskeletal organization through binding to ZRP-1, a member of the Lim family of proteins. J. Biol. Chem. 279:32858-32868.
    • (2004) J. Biol. Chem. , vol.279 , pp. 32858-32868
    • Sanz-Rodriguez, F.1    Guerrero-Esteo, M.2    Botella, L.M.3    Banville, D.4    Vary, C.P.5    Bernabeu, C.6
  • 37
    • 0037154212 scopus 로고    scopus 로고
    • Supervillin associates with androgen receptor and modulates its transcriptional activity
    • Ting, H.J., S. Yeh, K. Nishimura, and C. Chang. 2002. Supervillin associates with androgen receptor and modulates its transcriptional activity. Proc. Natl. Acad. Sci. USA. 99:661-666.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 661-666
    • Ting, H.J.1    Yeh, S.2    Nishimura, K.3    Chang, C.4
  • 38
    • 0347951044 scopus 로고    scopus 로고
    • The PDZ-LIM protein RIL modulates actin stress fiber turnover and enhances the association of alpha-actinin with F-actin
    • Vallenius, T., B. Scharm, A. Vesikansa, K. Luukko, R. Schafer, and T.P. Makela. 2004. The PDZ-LIM protein RIL modulates actin stress fiber turnover and enhances the association of alpha-actinin with F-actin. Exp. Cell Res. 293:117-128.
    • (2004) Exp. Cell Res. , vol.293 , pp. 117-128
    • Vallenius, T.1    Scharm, B.2    Vesikansa, A.3    Luukko, K.4    Schafer, R.5    Makela, T.P.6
  • 39
    • 0035938201 scopus 로고    scopus 로고
    • LIM domain protein Trip6 has a conserved nuclear export signal, nuclear targeting sequences, and multiple transactivation domains
    • Wang, Y., and T.D. Gilmore. 2001. LIM domain protein Trip6 has a conserved nuclear export signal, nuclear targeting sequences, and multiple transactivation domains. Biochim. Biophys. Acta. 1538:260-272.
    • (2001) Biochim. Biophys. Acta , vol.1538 , pp. 260-272
    • Wang, Y.1    Gilmore, T.D.2
  • 40
    • 0037441865 scopus 로고    scopus 로고
    • Zyxin and paxillin proteins: Focal adhesion plaque LIM domain proteins go nuclear
    • Wang, Y., and T.D. Gilmore. 2003. Zyxin and paxillin proteins: focal adhesion plaque LIM domain proteins go nuclear. Biochim. Biophys. Acta. 1593:115-120.
    • (2003) Biochim. Biophys. Acta , vol.1593 , pp. 115-120
    • Wang, Y.1    Gilmore, T.D.2
  • 42
    • 0031983016 scopus 로고    scopus 로고
    • Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: Intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth
    • Williams, J.M., G.C. Chen, L. Zhu, and R.F. Rest. 1998. Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth. Mol. Microbiol. 27:171-186.
    • (1998) Mol. Microbiol. , vol.27 , pp. 171-186
    • Williams, J.M.1    Chen, G.C.2    Zhu, L.3    Rest, R.F.4
  • 43
    • 0032820201 scopus 로고    scopus 로고
    • Domain analysis of supervillin, an F-actin bundling plasma membrane protein with functional nuclear localization signals
    • Wulfkuhle, J.D., I.E. Donina, N.H. Stark, R.K. Pope, K.N. Pestonjamasp, M.L. Niswonger, and E.J. Luna. 1999. Domain analysis of supervillin, an F-actin bundling plasma membrane protein with functional nuclear localization signals. J. Cell Sci. 112:2125-2136.
    • (1999) J. Cell Sci. , vol.112 , pp. 2125-2136
    • Wulfkuhle, J.D.1    Donina, I.E.2    Stark, N.H.3    Pope, R.K.4    Pestonjamasp, K.N.5    Niswonger, M.L.6    Luna, E.J.7
  • 44
    • 1642279290 scopus 로고    scopus 로고
    • TRIP6 enhances lysophosphatidic acid-induced cell migration by interacting with the lysophosphatidic acid 2 receptor
    • Xu, J., Y.J. Lai, W.C. Lin, and F.T. Lin. 2004. TRIP6 enhances lysophosphatidic acid-induced cell migration by interacting with the lysophosphatidic acid 2 receptor. J. Biol. Chem. 279:10459-10468.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10459-10468
    • Xu, J.1    Lai, Y.J.2    Lin, W.C.3    Lin, F.T.4
  • 45
    • 0032522147 scopus 로고    scopus 로고
    • The human TRIP6 gene encodes a LIM domain protein and maps to chromosome 7q22, a region associated with tumorigenesis
    • Yi, J., and M.C. Beckerle. 1998. The human TRIP6 gene encodes a LIM domain protein and maps to chromosome 7q22, a region associated with tumorigenesis. Genomics. 49:314-316.
    • (1998) Genomics , vol.49 , pp. 314-316
    • Yi, J.1    Beckerle, M.C.2
  • 46
    • 0037088609 scopus 로고    scopus 로고
    • Members of the Zyxin family of LIM proteins interact with members of the p130Cas family of signal transducers
    • Yi, J., S. Kloeker, C.C. Jensen, S. Bockholt, H. Honda, H. Hirai, and M.C. Beckerle. 2002. Members of the Zyxin family of LIM proteins interact with members of the p130Cas family of signal transducers. J. Biol. Chem. 277:9580-9589.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9580-9589
    • Yi, J.1    Kloeker, S.2    Jensen, C.C.3    Bockholt, S.4    Honda, H.5    Hirai, H.6    Beckerle, M.C.7
  • 47
    • 27544435992 scopus 로고    scopus 로고
    • Mechanical force mobilizes zyxin from focal adhesions to actin filaments and regulates cytoskeletal reinforcement
    • Yoshigi, M., L.M. Hoffman, C.C. Jensen, H.J. Yost, and M.C. Beckerle. 2005. Mechanical force mobilizes zyxin from focal adhesions to actin filaments and regulates cytoskeletal reinforcement. J. Cell Biol. 171:209-215.
    • (2005) J. Cell Biol. , vol.171 , pp. 209-215
    • Yoshigi, M.1    Hoffman, L.M.2    Jensen, C.C.3    Yost, H.J.4    Beckerle, M.C.5
  • 50
    • 0029858630 scopus 로고    scopus 로고
    • A zyxin-related protein whose synthesis is reduced in virally transformed fibroblasts
    • Zumbrunn, J., and B. Trueb. 1996. A zyxin-related protein whose synthesis is reduced in virally transformed fibroblasts. Eur. J. Biochem. 241:657-663.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 657-663
    • Zumbrunn, J.1    Trueb, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.