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Volumn 112, Issue 2, 1999, Pages 181-190

Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin

Author keywords

Fak; Focal adhesion; Integrin; LIM domain; Paxillin; Vinculin

Indexed keywords

CELL ADHESION MOLECULE; COMPLEMENTARY DNA; PAXILLIN; VINCULIN;

EID: 0033060357     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (136)

References (44)
  • 1
    • 0030024632 scopus 로고    scopus 로고
    • Specificity of single LIM motifs in targeting and LIM/LIM interactions in situ
    • Arber, S. and Caroni, P. (1996). Specificity of single LIM motifs in targeting and LIM/LIM interactions in situ. Genes Dev. 10, 289-300.
    • (1996) Genes Dev. , vol.10 , pp. 289-300
    • Arber, S.1    Caroni, P.2
  • 2
    • 0029166094 scopus 로고
    • Characterization of tyrosine phosphorylation of paxillin in vitro by focal adhesion kinase
    • Bellis, S. L., Miller, J. T. and Turner, C. E. (1995). Characterization of tyrosine phosphorylation of paxillin in vitro by focal adhesion kinase. J. Biol. Chem. 270, 17437-17441.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17437-17441
    • Bellis, S.L.1    Miller, J.T.2    Turner, C.E.3
  • 3
    • 0030793696 scopus 로고    scopus 로고
    • Adhesion of fibroblasts to fibronectin stimulates both serine and tyrosine phosphorylation of paxillin
    • Bellis, S. L., Perrotta, J. A., Curtis, M. S. and Turner, C. E. (1997). Adhesion of fibroblasts to fibronectin stimulates both serine and tyrosine phosphorylation of paxillin. Biochem. J. 325, 375-381.
    • (1997) Biochem. J. , vol.325 , pp. 375-381
    • Bellis, S.L.1    Perrotta, J.A.2    Curtis, M.S.3    Turner, C.E.4
  • 4
    • 0026658116 scopus 로고
    • Tyrosine-phosphorylated epidermal growth factor receptor and cellular p130 provide high affinity binding substrates to analyze Crk-phosphotyrosine-dependent interactions in vitro
    • Birge, R. B., Fajardo, J. E., Mayer, B. J. and Hanafusa, H. (1992). Tyrosine-phosphorylated epidermal growth factor receptor and cellular p130 provide high affinity binding substrates to analyze Crk-phosphotyrosine-dependent interactions in vitro. J. Biol. Chem. 267, 10588-10595.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10588-10595
    • Birge, R.B.1    Fajardo, J.E.2    Mayer, B.J.3    Hanafusa, H.4
  • 5
    • 0027219262 scopus 로고
    • Identification and characterization of a high-affinity interaction between v-Crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblasts
    • Birge, R. B., Fajardo, J. E., Reichman, C., Shoelson, S. E., Songyang, Z., et al, (1993). Identification and characterization of a high-affinity interaction between v-Crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblasts. Mol. Cell Biol. 13, 4648-4656.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 4648-4656
    • Birge, R.B.1    Fajardo, J.E.2    Reichman, C.3    Shoelson, S.E.4    Songyang, Z.5
  • 6
    • 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. and Turner, C. E. (1996). 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 135, 1109-1123.
    • (1996) J. Cell Biol , vol.135 , pp. 1109-1123
    • Brown, M.C.1    Perrotta, J.A.2    Turner, C.E.3
  • 7
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie, M., Tu, Y., Euskirchen, G., Ward, W. W. and Prasher, D. C. (1994). Green fluorescent protein as a marker for gene expression. Science 263, 802-805.
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 8
    • 0023392945 scopus 로고
    • High efficiency transformation of mammalian cells by plasmid DNA
    • Chen, C. and Okayama, H. (1987). High efficiency transformation of mammalian cells by plasmid DNA. Mol Cell. Biol. 7, 2745-2752.
    • (1987) Mol Cell. Biol. , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 9
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark, E. A. and Brugge, J. S. (1995). Integrins and signal transduction pathways: the road taken. Science 268, 233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 11
    • 0029976232 scopus 로고    scopus 로고
    • Integrin alpha v beta 5-dependent serine phosphorylation of paxillin in cultured human macrophages adherent to vitronectin
    • De Nichilo, M. O. and Yamada, K. M. (1996). Integrin alpha v beta 5-dependent serine phosphorylation of paxillin in cultured human macrophages adherent to vitronectin. J Biol. Chem. 271, 11016-11022.
    • (1996) J Biol. Chem. , vol.271 , pp. 11016-11022
    • De Nichilo, M.O.1    Yamada, K.M.2
  • 12
    • 0022340978 scopus 로고
    • Isolation of Monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evans, G., Lewis, G., Ramsey, G. and Bishop, J. (1985). Isolation of Monoclonal Antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol. 5, 3610-3616.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3610-3616
    • Evans, G.1    Lewis, G.2    Ramsey, G.3    Bishop, J.4
  • 13
    • 0024382542 scopus 로고
    • Novel tyrosine kinase substrates from Rous sarcoma virus-transformed cells are present in the membrane skeleton
    • Glenney, J. R. and Zokas, L. (1989). Novel tyrosine kinase substrates from Rous sarcoma virus-transformed cells are present in the membrane skeleton. J. Cell Biol. 108, 2401-2408.
    • (1989) J. Cell Biol. , vol.108 , pp. 2401-2408
    • Glenney, J.R.1    Zokas, L.2
  • 14
    • 0029055784 scopus 로고
    • Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase
    • Hildebrand, J. D., Schaller, M. D. and Parsons, J. T. (1995) Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase. Mol. Biol. Cell 6, 637-647.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 637-647
    • Hildebrand, J.D.1    Schaller, M.D.2    Parsons, J.T.3
  • 15
    • 0031044781 scopus 로고    scopus 로고
    • Focal adhesion kinase: At the crossroads of signal transduction
    • Ilie, D., Damsky, C. H. and Yamamoto, T. (1997). Focal adhesion kinase: at the crossroads of signal transduction. J. Cell Sci. 110, 401-407.
    • (1997) J. Cell Sci. , vol.110 , pp. 401-407
    • Ilie, D.1    Damsky, C.H.2    Yamamoto, T.3
  • 17
    • 0031002664 scopus 로고    scopus 로고
    • Monocyte cells and cancer cells express novel paxillin isoforms with different binding properties to focal adhesion proteins
    • Mazaki, Y., Hashimoto, S. and Sabe, H. (1997). Monocyte cells and cancer cells express novel paxillin isoforms with different binding properties to focal adhesion proteins. J. Biol. Chem. 272, 7437-7444.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7437-7444
    • Mazaki, Y.1    Hashimoto, S.2    Sabe, H.3
  • 18
    • 0030967789 scopus 로고    scopus 로고
    • Nuclear-cytoplasmic shuttling of the focal contact protein, zyxin: A potential mechanism for communication between sites of cell adhesion and the nucleus
    • Nix, D. A. and Beckerle, M. C. (1997). Nuclear-cytoplasmic shuttling of the focal contact protein, zyxin: a potential mechanism for communication between sites of cell adhesion and the nucleus. J. Cell Biol. 138, 1139-1147.
    • (1997) J. Cell Biol. , vol.138 , pp. 1139-1147
    • Nix, D.A.1    Beckerle, M.C.2
  • 19
    • 0029794722 scopus 로고    scopus 로고
    • Interactions between Src homology (SH) 2/SH3 adapter proteins and the guanylnucleotide exchange factor SOS are differentially regulated by insulin and epidermal growth factor
    • Okada, S. and Pessin, J. E. (1996). Interactions between Src homology (SH) 2/SH3 adapter proteins and the guanylnucleotide exchange factor SOS are differentially regulated by insulin and epidermal growth factor. J. Biol. Chem. 271, 25533-2558.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25533-32558
    • Okada, S.1    Pessin, J.E.2
  • 20
    • 0027971687 scopus 로고
    • Identification of Src, Fyn, Lyn, PI3K and Abl SH3 domain ligands using phage display libraries
    • Rickles, R. J., Botfield, M. C., Weng, Z., Taylor, J. A., Green, O. M., et al. (1994). Identification of Src, Fyn, Lyn, PI3K and Abl SH3 domain ligands using phage display libraries. EMBO J. 13, 5598-5604.
    • (1994) EMBO J. , vol.13 , pp. 5598-5604
    • Rickles, R.J.1    Botfield, M.C.2    Weng, Z.3    Taylor, J.A.4    Green, O.M.5
  • 21
    • 0028430196 scopus 로고
    • Maps from two interspecific backcross DNA panels available as a community genetic mapping resource
    • published erratum appears in Mamm Genome (1994) 5, 463
    • Rowe, L. B., Nadeau, J. H., Turner, R., Frankel, W. N., Letts, V. A., et al. (1994). Maps from two interspecific backcross DNA panels available as a community genetic mapping resource [published erratum appears in Mamm Genome (1994) 5, 463]. Mamm. Genome 5, 253-274.
    • (1994) Mamm. Genome , vol.5 , pp. 253-274
    • Rowe, L.B.1    Nadeau, J.H.2    Turner, R.3    Frankel, W.N.4    Letts, V.A.5
  • 22
    • 0028260229 scopus 로고
    • Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src
    • Sabe, H., Hata, A., Okada, M., Nakagawa, H. and Hanafusa, H. (1994). Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src. Proc. Nat. Acad. Sci. USA 91, 3984-3988.
    • (1994) Proc. Nat. Acad. Sci. USA , vol.91 , pp. 3984-3988
    • Sabe, H.1    Hata, A.2    Okada, M.3    Nakagawa, H.4    Hanafusa, H.5
  • 23
    • 0028875460 scopus 로고
    • Increased tyrosine phosphorylation of focal adhesion proteins in mycloid cell lines expressing p210BCR/ABL
    • Salgia, R., Brunkhorst, B., Pisick, E., Li, J. L., Lo, S. H., et al. (1995a). Increased tyrosine phosphorylation of focal adhesion proteins in mycloid cell lines expressing p210BCR/ABL. Oncogene 11, 1149-1155.
    • (1995) Oncogene , vol.11 , pp. 1149-1155
    • Salgia, R.1    Brunkhorst, B.2    Pisick, E.3    Li, J.L.4    Lo, S.H.5
  • 24
    • 0028925737 scopus 로고
    • Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by P210BCR/ABL
    • Salgia, R., Li, J. L., Lo, S. H., Brunkhorst, B., Kansas, G. S., et al. (1995b). Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by P210BCR/ABL. J. Biol. Chem. 270, 5039-5047.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5039-5047
    • Salgia, R.1    Li, J.L.2    Lo, S.H.3    Brunkhorst, B.4    Kansas, G.S.5
  • 26
    • 0027439594 scopus 로고
    • Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK
    • Schaller, M. D., Borgman, C. A. and Parsons, J. T. (1993). Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK. Mol. Cell Biol. 13, 785-791.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 785-791
    • Schaller, M.D.1    Borgman, C.A.2    Parsons, J.T.3
  • 27
    • 0028986116 scopus 로고
    • Pp125FAK-dependent tyrosine phosphorylation of puxillin creates a high-affinity binding site for Crk
    • Schaller, M. D. and Parsons, J. T. (1995) pp125FAK-dependent tyrosine phosphorylation of puxillin creates a high-affinity binding site for Crk. Mol. Cell Biol. 15, 2635-2645.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 2635-2645
    • Schaller, M.D.1    Parsons, J.T.2
  • 29
    • 0028134697 scopus 로고
    • The LIM domain is a modular protein-binding interface
    • Schmeichel, K. L. and Beckerle, M. C. (1994) The LIM domain is a modular protein-binding interface. Cell 79, 211-219.
    • (1994) Cell , vol.79 , pp. 211-219
    • Schmeichel, K.L.1    Beckerle, M.C.2
  • 31
    • 0028171070 scopus 로고
    • Characterization of the TGF beta 1-inducible hic-5 gene that encodes a putative novel zinc finger protein and its possible involvement in cellular senescence
    • Shibanuma, M., Mashimo, J., Kuroki, T. and Nose, K. (1994). Characterization of the TGF beta 1-inducible hic-5 gene that encodes a putative novel zinc finger protein and its possible involvement in cellular senescence. J. Biol. Chem. 269, 26767-26774.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26767-26774
    • Shibanuma, M.1    Mashimo, J.2    Kuroki, T.3    Nose, K.4
  • 32
    • 0031027206 scopus 로고    scopus 로고
    • Induction of senescence-like phenotypes by forced expression of hic-5, which encodes a novel LIM motif protein, in immortalized human fibroblasts
    • Shibanuma, M., Mochizuki, E., Maniwa, R., Mashimo, J., Nishiya, N., et al. (1997). Induction of senescence-like phenotypes by forced expression of hic-5, which encodes a novel LIM motif protein, in immortalized human fibroblasts. Mol. Cell Biol. 17, 1224-1235.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 1224-1235
    • Shibanuma, M.1    Mochizuki, E.2    Maniwa, R.3    Mashimo, J.4    Nishiya, N.5
  • 33
    • 0027403027 scopus 로고
    • SH2 domains recognize specific phosphopeptide sequences
    • Songyang, Z., Shoelson, S. E., Chaudhuri, M., Gish, G., Pawson, T., et al. (1993). SH2 domains recognize specific phosphopeptide sequences. Cell 72, 767-778.
    • (1993) Cell , vol.72 , pp. 767-778
    • Songyang, Z.1    Shoelson, S.E.2    Chaudhuri, M.3    Gish, G.4    Pawson, T.5
  • 34
    • 0028351583 scopus 로고
    • Specific motifs recognized by the SH2 domains of Csk. 3BP2, fps/fes, GRB-2. HCP. SHC. Syk, and Vav
    • Songjang, Z., Shoelson, S. E., McGlade, J., Olivier, P., Pawson, T., et al. (1994). Specific motifs recognized by the SH2 domains of Csk. 3BP2, fps/fes, GRB-2. HCP. SHC. Syk, and Vav. Mol. Cell Biol. 14, 2777-2785.
    • (1994) Mol. Cell Biol. , vol.14 , pp. 2777-2785
    • Songjang, Z.1    Shoelson, S.E.2    McGlade, J.3    Olivier, P.4    Pawson, T.5
  • 35
    • 0029045815 scopus 로고
    • Specific and redundant roles of Src and Fyn in organizing the cytoskeleton
    • Thomas, S. M., Soriano, P. and Imamoto, A. (1995). Specific and redundant roles of Src and Fyn in organizing the cytoskeleton. Nature 376, 267-271.
    • (1995) Nature , vol.376 , pp. 267-271
    • Thomas, S.M.1    Soriano, P.2    Imamoto, A.3
  • 36
    • 0031001560 scopus 로고    scopus 로고
    • The bovine papillomavirus E6 oncoprotein interacts with paxillin and disrupts the actin cytoskeleton
    • Tong, X. and Howley, P. M. (1997). The bovine papillomavirus E6 oncoprotein interacts with paxillin and disrupts the actin cytoskeleton. Proc. Nat. Acad. Sci. USA 94, 4412-4417.
    • (1997) Proc. Nat. Acad. Sci. USA , vol.94 , pp. 4412-4417
    • Tong, X.1    Howley, P.M.2
  • 37
    • 0031439110 scopus 로고    scopus 로고
    • The bovine papillomavirus E6 protein binds to the LD motif repeats of paxillin and blocks its interaction with vinculin and the focal adhesion kinase
    • Tong, X., Salgia, R., Li, J. L., Griffin, J. D. and Howley, P. M. (1997). The bovine papillomavirus E6 protein binds to the LD motif repeats of paxillin and blocks its interaction with vinculin and the focal adhesion kinase [In Process Citation]. J. Biol. Chem. 272, 33373-33376.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33373-33376
    • Tong, X.1    Salgia, R.2    Li, J.L.3    Griffin, J.D.4    Howley, P.M.5
  • 38
    • 0025008074 scopus 로고
    • Paxillin: A new vinculin-binding protein present in focal adhesions
    • Turner, C. E., Glenney, J. R. J. and Burridge, K. (1990). Paxillin: a new vinculin-binding protein present in focal adhesions. J. Cell Biol. 111, 1059-68.
    • (1990) J. Cell Biol. , vol.111 , pp. 1059-1068
    • Turner, C.E.1    Glenney, J.R.J.2    Burridge, K.3
  • 39
    • 0027966390 scopus 로고
    • Paxillin: A cytoskeletal target for tyrosine kinases
    • Turner, C. E. (1994). Paxillin: a cytoskeletal target for tyrosine kinases. BioEssays 16, 47-52.
    • (1994) BioEssays , vol.16 , pp. 47-52
    • Turner, C.E.1
  • 40
    • 0028289562 scopus 로고
    • Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: Identification of a vinculin and pp125Fak-binding region
    • Turner, C. E. and Miller, J. T. (1994). Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: identification of a vinculin and pp125Fak-binding region. J. Cell Sci.
    • (1994) J. Cell Sci.
    • Turner, C.E.1    Miller, J.T.2
  • 41
    • 0032495590 scopus 로고    scopus 로고
    • Association of papillomavirus E6 oncoproteins with the focal adhesion protein paxillin through a conserved protein interaction motif
    • in press
    • Vande Pol, S. B., Brown, M. C. and Turner, C. E. (1998). Association of papillomavirus E6 oncoproteins with the focal adhesion protein paxillin through a conserved protein interaction motif. Oncogene (in press).
    • (1998) Oncogene
    • Vande Pol, S.B.1    Brown, M.C.2    Turner, C.E.3
  • 42
    • 0027293670 scopus 로고
    • Detection of Src homology 3-binding proteins, including paxillin, in normal and v-Src-transformed Balb/c 3T3 cells
    • Weng, Z., Tajlor, J. A., Turner, C. E., Brugge, J. S. and Seidel, D. C. (1993). Detection of Src homology 3-binding proteins, including paxillin, in normal and v-Src-transformed Balb/c 3T3 cells. J. Biol. Chem. 268, 14956-14963.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14956-14963
    • Weng, Z.1    Tajlor, J.A.2    Turner, C.E.3    Brugge, J.S.4    Seidel, D.C.5
  • 43
    • 0030777767 scopus 로고    scopus 로고
    • Induction of apoptosis after expression of PYK2, a tyrosine kinase structurally related to focal adhesion kinase
    • Xiong, W. and Parsons, J. T. (1997). Induction of apoptosis after expression of PYK2, a tyrosine kinase structurally related to focal adhesion kinase. J. Cell Biol. 139, 529-539.
    • (1997) J. Cell Biol. , vol.139 , pp. 529-539
    • Xiong, W.1    Parsons, J.T.2
  • 44
    • 0030990991 scopus 로고    scopus 로고
    • Disruption of overlapping transcripts in the ROSA beta geo 26 gene trap strain leads to widespread expression of beta-galactosidase in mouse embryos and hematopoietic cells
    • Zambrowicz, B. P., Imamoto, A., Fiering, S., Herzenberg, L. A., Kerr, W. G. and Soriano, P. (1997). Disruption of overlapping transcripts in the ROSA beta geo 26 gene trap strain leads to widespread expression of beta-galactosidase in mouse embryos and hematopoietic cells. Proc. Nat. Acad. Sci. USA 94, 3789-3794.
    • (1997) Proc. Nat. Acad. Sci. USA , vol.94 , pp. 3789-3794
    • Zambrowicz, B.P.1    Imamoto, A.2    Fiering, S.3    Herzenberg, L.A.4    Kerr, W.G.5    Soriano, P.6


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