메뉴 건너뛰기




Volumn 197, Issue 2, 2003, Pages 297-305

Reduced Cell Adhesion during Mitosis by Threonine Phosphorylation of β1 Integrin

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; BETA1 INTEGRIN; BLOCKING ANTIBODY; INTEGRIN; LAMININ; PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEIN KINASE (CALCIUM,CALMODULIN) II; SERINE THREONINE PROTEIN PHOSPHATASE 2A; THREONINE; UNCLASSIFIED DRUG; ANTIBODY; CALMODULIN DEPENDENT PROTEIN KINASE II; CALMODULIN-DEPENDENT PROTEIN KINASE II; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN KINASE (CALCIUM,CALMODULIN);

EID: 0242317411     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/jcp.10354     Document Type: Article
Times cited : (41)

References (35)
  • 1
    • 0029085160 scopus 로고
    • The cardiac sarcoplasmic reticulum phospholamban kinase is a distinct δ-CaM kinase isozyme
    • Baltas LG, Karczewski P, Krause EG. 1995. The cardiac sarcoplasmic reticulum phospholamban kinase is a distinct δ-CaM kinase isozyme. FEBS Lett 373:71-75.
    • (1995) FEBS Lett , vol.373 , pp. 71-75
    • Baltas, L.G.1    Karczewski, P.2    Krause, E.G.3
  • 2
    • 0023691731 scopus 로고
    • Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics
    • Bialojan C, Takai A. 1988. Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics. Biochem J 256:283-290.
    • (1988) Biochem J , vol.256 , pp. 283-290
    • Bialojan, C.1    Takai, A.2
  • 3
    • 0030612268 scopus 로고    scopus 로고
    • Requirement of integrin β3 tyrosine 747 for β3 tyrosine phosphorylation and regulation of αvβ3 avidity
    • Blystone SD, Williams MP, Slater SE, Brown EJ. 1997. Requirement of integrin β3 tyrosine 747 for β3 tyrosine phosphorylation and regulation of αvβ3 avidity. J Biol Chem 272:28757-28761.
    • (1997) J Biol Chem , vol.272 , pp. 28757-28761
    • Blystone, S.D.1    Williams, M.P.2    Slater, S.E.3    Brown, E.J.4
  • 4
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and cytoskeleton
    • Burridge K, Fath K, Kelly T, Nuckolls G, Turner C. 1988. Focal adhesions: transmembrane junctions between the extracellular matrix and cytoskeleton. Annu Rev Cell Biol 4:487-525.
    • (1988) Annu Rev Cell Biol , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, G.4    Turner, C.5
  • 5
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen P. 1989. The structure and regulation of protein phosphatases. Annu Rev Biochem 58:453-508.
    • (1989) Annu Rev Biochem , vol.58 , pp. 453-508
    • Cohen, P.1
  • 6
    • 0018140371 scopus 로고
    • Role of cell shape in growth control
    • Folkman J, Moscona A. 1978. Role of cell shape in growth control. Nature 273:345-349.
    • (1978) Nature , vol.273 , pp. 345-349
    • Folkman, J.1    Moscona, A.2
  • 7
    • 0027445508 scopus 로고
    • Proteins associated with the cytoplasmic surface of adhesion molecules
    • Gumbiner BM. 1993. Proteins associated with the cytoplasmic surface of adhesion molecules. Neuron 11:551-564.
    • (1993) Neuron , vol.11 , pp. 551-564
    • Gumbiner, B.M.1
  • 8
    • 0345178412 scopus 로고
    • Serum-free growth of human mammary epithelial cells: Rapid clonal growth in define medium and extended serial passage with pituitary extract
    • Hammond SL, Ham RG, Stampfer MR. 1984. Serum-free growth of human mammary epithelial cells: Rapid clonal growth in define medium and extended serial passage with pituitary extract. Proc Natl Acad Sci USA 81:5435-5439.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 5435-5439
    • Hammond, S.L.1    Ham, R.G.2    Stampfer, M.R.3
  • 10
    • 0022534722 scopus 로고
    • Interaction of plasma membrane fibronectin receptor with talin-A transmembrane receptor
    • Horwitz A, Duggan E, Buck C, Beckerle MC, Burridge K. 1986. Interaction of plasma membrane fibronectin receptor with talin-A transmembrane receptor. Nature 320:531-533.
    • (1986) Nature , vol.320 , pp. 531-533
    • Horwitz, A.1    Duggan, E.2    Buck, C.3    Beckerle, M.C.4    Burridge, K.5
  • 11
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes RO. 1992. Integrins: Versatility, modulation, and signaling in cell adhesion. Cell 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 12
    • 0033378656 scopus 로고    scopus 로고
    • Integrin-linked kinase is localized to cell-matrix focal adhesions but not in cell-cell adhesion sites and the focal adhesion localization of integrin-linked kinase is regulated by the PINCH-binding ANK repeats
    • Li F, Zhang Y, Wu C. 1999. Integrin-linked kinase is localized to cell-matrix focal adhesions but not in cell-cell adhesion sites and the focal adhesion localization of integrin-linked kinase is regulated by the PINCH-binding ANK repeats. J Cell Sci 112:4589-4599.
    • (1999) J Cell Sci , vol.112 , pp. 4589-4599
    • Li, F.1    Zhang, Y.2    Wu, C.3
  • 13
    • 0034238109 scopus 로고    scopus 로고
    • Phosphorylation of the β1 integrin cytoplasmic domain: Toward and understanding of function and mechanism
    • Mulrooney J, Foley K, Vineberg S, Barreuther M, Grabel L. 2000. Phosphorylation of the β1 integrin cytoplasmic domain: Toward and understanding of function and mechanism. Exp Cell Res 258:332-341.
    • (2000) Exp Cell Res , vol.258 , pp. 332-341
    • Mulrooney, J.1    Foley, K.2    Vineberg, S.3    Barreuther, M.4    Grabel, L.5
  • 14
    • 0034928398 scopus 로고    scopus 로고
    • Serine 785 phosphorylation of the β1 cytoplasmic domain modulates β1A-integrin-dependent functions
    • Mulrooney JP, Hong T, Grabel LB. 2001. Serine 785 phosphorylation of the β1 cytoplasmic domain modulates β1A-integrin-dependent functions. J Cell Sci 114:2525-2533.
    • (2001) J Cell Sci , vol.114 , pp. 2525-2533
    • Mulrooney, J.P.1    Hong, T.2    Grabel, L.B.3
  • 15
    • 0027143725 scopus 로고
    • Protein serine/threonine phosphatases: Structure, regulation, and functions in cell growth
    • Mumby MC, Walter G. 1993. Protein serine/threonine phosphatases: Structure, regulation, and functions in cell growth. Physiol Rev 73:673-699.
    • (1993) Physiol Rev , vol.73 , pp. 673-699
    • Mumby, M.C.1    Walter, G.2
  • 16
    • 0025291522 scopus 로고
    • An interaction between α-actinin and the β1 integrin subunit in vitro
    • Otey CA, Pavalko FM, Burridge K. 1990. An interaction between α-actinin and the β1 integrin subunit in vitro. J Cell Biol 111:721-729.
    • (1990) J Cell Biol , vol.111 , pp. 721-729
    • Otey, C.A.1    Pavalko, F.M.2    Burridge, K.3
  • 17
    • 0028351295 scopus 로고
    • Role of adhesion molecule cytoplasmic domains in mediating interactions with the cytoskeleton
    • Pavalko FM, Otey CA. 1994. Role of adhesion molecule cytoplasmic domains in mediating interactions with the cytoskeleton. Proc Soc Exp Biol Med 205:282-293.
    • (1994) Proc Soc Exp Biol Med , vol.205 , pp. 282-293
    • Pavalko, F.M.1    Otey, C.A.2
  • 18
    • 0028919214 scopus 로고
    • Modulation of cell adhesion by changes in αLβ2 (LFA-1, CD11a/CD18) cytoplasmic domain/cytoskeleton interaction
    • Peter K, O'Toole TE. 1995. Modulation of cell adhesion by changes in αLβ2 (LFA-1, CD11a/CD18) cytoplasmic domain/cytoskeleton interaction. J Exp Med 181:315-326.
    • (1995) J Exp Med , vol.181 , pp. 315-326
    • Peter, K.1    O'Toole, T.E.2
  • 19
    • 0032549860 scopus 로고    scopus 로고
    • Modulation of β1A integrin functions by tyrosine residues in the β1 cytoplasmic domain
    • Sakai T, Zhang Q, Fassler R, Mosher DF. 1998. Modulation of β1A integrin functions by tyrosine residues in the β1 cytoplasmic domain. J Cell Biol 141:527-538.
    • (1998) J Cell Biol , vol.141 , pp. 527-538
    • Sakai, T.1    Zhang, Q.2    Fassler, R.3    Mosher, D.F.4
  • 21
    • 0014418101 scopus 로고
    • Anchorage and growth regulation in normal and virus-transformed cells
    • Stoker M, O'Neill C, Berryman S, Waxman V. 1968. Anchorage and growth regulation in normal and virus-transformed cells. Int J Cancer 3:683-693.
    • (1968) Int J Cancer , vol.3 , pp. 683-693
    • Stoker, M.1    O'Neill, C.2    Berryman, S.3    Waxman, V.4
  • 22
    • 0034708070 scopus 로고    scopus 로고
    • Cytoplasmic domain mutants of β1 integrin, expressed in β1-knockout lymphoma cells, have distinct effects on adhesion, invasion and metastasis
    • Stroeken PJM, van Rijthoven EAM, de Boer E, Geerts D, Roos E. 2000. Cytoplasmic domain mutants of β1 integrin, expressed in β1-knockout lymphoma cells, have distinct effects on adhesion, invasion and metastasis. Oncogene 19:1232-1238.
    • (2000) Oncogene , vol.19 , pp. 1232-1238
    • Stroeken, P.J.M.1    Van Rijthoven, E.A.M.2    De Boer, E.3    Geerts, D.4    Roos, E.5
  • 23
    • 0033127162 scopus 로고    scopus 로고
    • Reduced substratum adhesion and decreased expressions of β1 and β4 integrins in human breast cancer cells with a property of anchorage-independent growth
    • Suzuki K, Takahashi K. 1999. Reduced substratum adhesion and decreased expressions of β1 and β4 integrins in human breast cancer cells with a property of anchorage-independent growth. Int J Oncol 14:897-904.
    • (1999) Int J Oncol , vol.14 , pp. 897-904
    • Suzuki, K.1    Takahashi, K.2
  • 24
    • 0034835245 scopus 로고    scopus 로고
    • Actin filament assembly and actinmyosin contractility are necessary for anchorage- and EGF-dependent activation of phospholipase Cγ
    • Suzuki K, Takahashi K. 2001. Actin filament assembly and actinmyosin contractility are necessary for anchorage- and EGF-dependent activation of phospholipase Cγ. J Cell Physiol 189:64-71.
    • (2001) J Cell Physiol , vol.189 , pp. 64-71
    • Suzuki, K.1    Takahashi, K.2
  • 25
    • 2342607440 scopus 로고    scopus 로고
    • The linkage between β1 integrin and the actin cytoskeleton is differentially regulated by tyrosine and serine/ threonine phosphorylation of β1 integrin in normal and cancerous human breast cells
    • Takahashi K. 2001. The linkage between β1 integrin and the actin cytoskeleton is differentially regulated by tyrosine and serine/ threonine phosphorylation of β1 integrin in normal and cancerous human breast cells. BMC Cell Biol 2:23 (http://www.biomedcentral.com/1471-2121/2/23).
    • (2001) BMC Cell Biol , vol.2 , pp. 23
    • Takahashi, K.1
  • 26
    • 0030578460 scopus 로고    scopus 로고
    • Density-dependent inhibition of growth involves prevention of EGF receptor activation by E-cadherin mediated cell-cell adhesion
    • Takahashi K, Suzuki K. 1996. Density-dependent inhibition of growth involves prevention of EGF receptor activation by E-cadherin mediated cell-cell adhesion. Exp Cell Res 226:214-222.
    • (1996) Exp Cell Res , vol.226 , pp. 214-222
    • Takahashi, K.1    Suzuki, K.2
  • 27
    • 0030847274 scopus 로고    scopus 로고
    • Induction of tyrosine phosphorylation and association of β-catenin with EGF receptor upon tryptic digestion of quiescent cells at confluence
    • Takahashi K, Suzuki K, Tsukatani Y. 1997. Induction of tyrosine phosphorylation and association of β-catenin with EGF receptor upon tryptic digestion of quiescent cells at confluence. Oncogene 15:71-78.
    • (1997) Oncogene , vol.15 , pp. 71-78
    • Takahashi, K.1    Suzuki, K.2    Tsukatani, Y.3
  • 30
    • 0030833223 scopus 로고    scopus 로고
    • Loss of density-dependent growth inhibition and dissociation of α-catenin from E-cadherin
    • Tsukatani Y, Suzuki K, Takahashi K. 1997. Loss of density-dependent growth inhibition and dissociation of α-catenin from E-cadherin. J Cell Physiol 173:54-63.
    • (1997) J Cell Physiol , vol.173 , pp. 54-63
    • Tsukatani, Y.1    Suzuki, K.2    Takahashi, K.3
  • 31
    • 0023871140 scopus 로고
    • Three distinct forms of type 2A protein phosphatase in human erythrocyte cytosol
    • Usui H, Imazu M, Maeta K, Tsukamoto H, Azuma K, Takeda M. 1988. Three distinct forms of type 2A protein phosphatase in human erythrocyte cytosol. J Biol Chem 263:3752-3762.
    • (1988) J Biol Chem , vol.263 , pp. 3752-3762
    • Usui, H.1    Imazu, M.2    Maeta, K.3    Tsukamoto, H.4    Azuma, K.5    Takeda, M.6
  • 32
    • 0029148897 scopus 로고
    • Treatment with okadaic acid reveals strong threonine phosphorylation of CD18 after activation of CD11/CD18 leukocyte integrins with phorbol esters or CD3 antibodies
    • Valmu L, Gahmberg CG. 1995. Treatment with okadaic acid reveals strong threonine phosphorylation of CD18 after activation of CD11/CD18 leukocyte integrins with phorbol esters or CD3 antibodies. J Immunol 155:1175-1183.
    • (1995) J Immunol , vol.155 , pp. 1175-1183
    • Valmu, L.1    Gahmberg, C.G.2
  • 33
    • 0033118404 scopus 로고    scopus 로고
    • Characterization of β2 (CD18) integrin phosphorylation in phorbol ester-activated T lymphocytes
    • Valmu L, Hilden TJ, van Willigen G, Gahmberg CG. 1999. Characterization of β2 (CD18) integrin phosphorylation in phorbol ester-activated T lymphocytes. Biochem J 339:119-125.
    • (1999) Biochem J , vol.339 , pp. 119-125
    • Valmu, L.1    Hilden, T.J.2    Van Willigen, G.3    Gahmberg, C.G.4
  • 34
    • 2642683511 scopus 로고    scopus 로고
    • Mutational analysis of the potential phosphorylation sites in the cytoplasmic domain of integrin β1A: Requirement for threonines 788-789 in receptor activation
    • Wennerberg K, Fassler R, Warmegaard B, Johansson S. 1998. Mutational analysis of the potential phosphorylation sites in the cytoplasmic domain of integrin β1A: Requirement for threonines 788-789 in receptor activation. J Cell Sci 111:1117-1126.
    • (1998) J Cell Sci , vol.111 , pp. 1117-1126
    • Wennerberg, K.1    Fassler, R.2    Warmegaard, B.3    Johansson, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.