메뉴 건너뛰기




Volumn 205, Issue 3, 2005, Pages 402-413

Cytoskeletal remodeling in vascular smooth muscle cells in response to angiotensin II-induced activation of the SHP-2 tyrosine phosphatase

Author keywords

[No Author keywords available]

Indexed keywords

ANGIOTENSIN; CELL PROTEIN; CRK ASSOCIATED SUBSTRATE PROTEIN; FOCAL ADHESION ASSOCIATED PROTEIN; MUTANT PROTEIN; OCTAPEPTIDE; PAXILLIN; PROTEIN P130; PROTEIN TYROSINE PHOSPHATASE SHP 2; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; TENSIN; UNCLASSIFIED DRUG; VAV PROTEIN; VAV2 PROTEIN;

EID: 27744499005     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/jcp.20436     Document Type: Article
Times cited : (16)

References (41)
  • 1
    • 0034269240 scopus 로고    scopus 로고
    • Structural basis for relief of autoinhibition of the Dbl homology domain of proto-oncogene Vav by tyrosine phosphorylation
    • Aghazadeh B, Lowry WE, Huang XY, Rosen MK. 2000. Structural basis for relief of autoinhibition of the Dbl homology domain of proto-oncogene Vav by tyrosine phosphorylation. Cell 102(5):625-633.
    • (2000) Cell , vol.102 , Issue.5 , pp. 625-633
    • Aghazadeh, B.1    Lowry, W.E.2    Huang, X.Y.3    Rosen, M.K.4
  • 2
    • 0033773347 scopus 로고    scopus 로고
    • Rho plays an important role in angiotensin II-induced hypertrophic responses in cardiac myocytes
    • Aikawa R, Komuro I, Nagai R, Yazaki Y. 2000. Rho plays an important role in angiotensin II-induced hypertrophic responses in cardiac myocytes. Mol Cell Biochem 212(1-2):177-182.
    • (2000) Mol Cell Biochem , vol.212 , Issue.1-2 , pp. 177-182
    • Aikawa, R.1    Komuro, I.2    Nagai, R.3    Yazaki, Y.4
  • 3
    • 0030874924 scopus 로고    scopus 로고
    • Dependence on the motif YIPP for the physical association of Jak2 kinase with the intracellular carboxyl tail of the angiotensin II AT1 receptor
    • Ali MS, Sayeski PP, Dirksen LB, Hayzer DJ, Marrero MB, Bernstein KE. 1997a. Dependence on the motif YIPP for the physical association of Jak2 kinase with the intracellular carboxyl tail of the angiotensin II AT1 receptor. J Biol Chem 272(37):23382-23388.
    • (1997) J Biol Chem , vol.272 , Issue.37 , pp. 23382-23388
    • Ali, M.S.1    Sayeski, P.P.2    Dirksen, L.B.3    Hayzer, D.J.4    Marrero, M.B.5    Bernstein, K.E.6
  • 4
    • 0030946253 scopus 로고    scopus 로고
    • Angiotensin II stimulates tyrosine phosphorylation and activation of insulin receptor substrate 1 and protein-tyrosine phosphatase ID in vascular smooth muscle cells
    • Ali MS, Schleifer B, Delafontaine P, Bernstein KE, Ling BN, Marrero MB. 1997b. Angiotensin II stimulates tyrosine phosphorylation and activation of insulin receptor substrate 1 and protein-tyrosine phosphatase ID in vascular smooth muscle cells. J Biol Chem 272(19):12373-12379.
    • (1997) J Biol Chem , vol.272 , Issue.19 , pp. 12373-12379
    • Ali, M.S.1    Schleifer, B.2    Delafontaine, P.3    Bernstein, K.E.4    Ling, B.N.5    Marrero, M.B.6
  • 5
    • 0034686082 scopus 로고    scopus 로고
    • Jak2 acts as both a STAT1 kinase and as a molecular bridge linking STAT1 to the angiotensin II AT1 receptor
    • Ali MS, Sayeski PP, Bernstein KE. 2000. Jak2 acts as both a STAT1 kinase and as a molecular bridge linking STAT1 to the angiotensin II AT1 receptor. J Biol Chem 275(20):15586-15593.
    • (2000) J Biol Chem , vol.275 , Issue.20 , pp. 15586-15593
    • Ali, M.S.1    Sayeski, P.P.2    Bernstein, K.E.3
  • 6
    • 0032489871 scopus 로고    scopus 로고
    • Angiotensin II activates RhoA in cardiac myocytes: A critical role of RhoA in angiotensin II-induced premyofibril formation
    • Aoki H, Izumo S, Sadoshima J. 1998. Angiotensin II activates RhoA in cardiac myocytes: A critical role of RhoA in angiotensin II-induced premyofibril formation. Circ Res 82(6):666-676.
    • (1998) Circ Res , vol.82 , Issue.6 , pp. 666-676
    • Aoki, H.1    Izumo, S.2    Sadoshima, J.3
  • 7
    • 0036088773 scopus 로고    scopus 로고
    • Inhibition of ERK attenuates force development by lowering myosin light chain phosphorylation
    • D'Angelo G, Adam LP. 2002. Inhibition of ERK attenuates force development by lowering myosin light chain phosphorylation. Am J Physiol Heart Circ Physiol 282(2):H602-610.
    • (2002) Am J Physiol Heart Circ Physiol , vol.282 , Issue.2
    • D'Angelo, G.1    Adam, L.P.2
  • 8
    • 0346996442 scopus 로고    scopus 로고
    • Selective down-regulation of angiotensin II receptor type 1A signaling by protein tyrosine phosphatase SHP-2 in vascular smooth muscle cells
    • Doan T, Farmer P, Cooney T, Ali MS. 2004. Selective down-regulation of angiotensin II receptor type 1A signaling by protein tyrosine phosphatase SHP-2 in vascular smooth muscle cells. Cell Signal 16(3):301-311.
    • (2004) Cell Signal , vol.16 , Issue.3 , pp. 301-311
    • Doan, T.1    Farmer, P.2    Cooney, T.3    Ali, M.S.4
  • 9
    • 0037075815 scopus 로고    scopus 로고
    • SHP-2 is involved in heterodimer specific loss of phosphorylation of Tyr771 in the PDGF beta-receptor
    • Ekman S, Kallin A, Engstrom U, Heldin CH, Ronnstrand L. 2002. SHP-2 is involved in heterodimer specific loss of phosphorylation of Tyr771 in the PDGF beta-receptor. Oncogene 21(12):1870-1875.
    • (2002) Oncogene , vol.21 , Issue.12 , pp. 1870-1875
    • Ekman, S.1    Kallin, A.2    Engstrom, U.3    Heldin, C.H.4    Ronnstrand, L.5
  • 10
    • 0032482171 scopus 로고    scopus 로고
    • The phosphotyrosine phosphatase SHP-2 participates in a multimeric signaling complex and regulates T cell receptor (TCR) coupling to the Ras/mitogen-activated protein kinase (MAPK) pathway in Jurkat T cells
    • Frearson JA, Alexander DR. 1998. The phosphotyrosine phosphatase SHP-2 participates in a multimeric signaling complex and regulates T cell receptor (TCR) coupling to the Ras/mitogen-activated protein kinase (MAPK) pathway in Jurkat T cells. J Exp Med 187(9):1417-1426.
    • (1998) J Exp Med , vol.187 , Issue.9 , pp. 1417-1426
    • Frearson, J.A.1    Alexander, D.R.2
  • 11
    • 0030753474 scopus 로고    scopus 로고
    • Association of PTP-PEST with the SH3 domain of p130cas; a novel mechanism of protein tyrosine phosphatase substrate recognition
    • Garton AJ, Burnham MR, Bouton AH, Tonks NK. 1997. Association of PTP-PEST with the SH3 domain of p130cas; a novel mechanism of protein tyrosine phosphatase substrate recognition. Oncogene 15(8):877-885.
    • (1997) Oncogene , vol.15 , Issue.8 , pp. 877-885
    • Garton, A.J.1    Burnham, M.R.2    Bouton, A.H.3    Tonks, N.K.4
  • 12
    • 0034714318 scopus 로고    scopus 로고
    • The protein-tyrosine phosphatase SHP-2 is required during angiotensin II-mediated activation of cyclin D1 promoter in CHO-AT1A cells
    • Guillemot L, Levy A, Zhao ZJ, Bereziat G, Rothhut B. 2000. The protein-tyrosine phosphatase SHP-2 is required during angiotensin II-mediated activation of cyclin D1 promoter in CHO-AT1A cells. J Biol Chem 275(34) 26349-26358.
    • (2000) J Biol Chem , vol.275 , Issue.34 , pp. 26349-26358
    • Guillemot, L.1    Levy, A.2    Zhao, Z.J.3    Bereziat, G.4    Rothhut, B.5
  • 13
    • 7244231301 scopus 로고    scopus 로고
    • MAP kinases and cell migration
    • Huang C, Jacobson K, Schaller MD. 2004. MAP kinases and cell migration. J Cell Sci 117(Pt 20):4619-4628.
    • (2004) J Cell Sci , vol.117 , Issue.PART 20 , pp. 4619-4628
    • Huang, C.1    Jacobson, K.2    Schaller, M.D.3
  • 15
    • 0034610777 scopus 로고    scopus 로고
    • Roles for the protein tyrosine phosphatase SHP-2 in cytoskeletal organization, cell adhesion and cell migration revealed by overexpression of a dominant negative mutant
    • Inagaki K, Noguchi T, Matozaki T, Horikawa T, Fukunaga K, Tsuda M, Ichihashi M, Kasuga M. 2000. Roles for the protein tyrosine phosphatase SHP-2 in cytoskeletal organization, cell adhesion and cell migration revealed by overexpression of a dominant negative mutant. Oncogene 19(1):75-84.
    • (2000) Oncogene , vol.19 , Issue.1 , pp. 75-84
    • Inagaki, K.1    Noguchi, T.2    Matozaki, T.3    Horikawa, T.4    Fukunaga, K.5    Tsuda, M.6    Ichihashi, M.7    Kasuga, M.8
  • 16
    • 0032576702 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase 1B negatively regulates integrin signaling
    • Liu F, Sells MA, Chernoff J. 1998. Protein tyrosine phosphatase 1B negatively regulates integrin signaling. Curr Biol 8(3):173-176.
    • (1998) Curr Biol , vol.8 , Issue.3 , pp. 173-176
    • Liu, F.1    Sells, M.A.2    Chernoff, J.3
  • 18
    • 15644368839 scopus 로고    scopus 로고
    • The COOH-terminal tyrosine phosphorylation sites on IRS-1 bind SHP-2 and negatively regulate insulin signaling
    • Myers MG, Jr, Mendez R, Shi P, Pierce JH, Rhoads R, White MF. 1998. The COOH-terminal tyrosine phosphorylation sites on IRS-1 bind SHP-2 and negatively regulate insulin signaling. J Biol Chem 273(41):26908-26914.
    • (1998) J Biol Chem , vol.273 , Issue.41 , pp. 26908-26914
    • Myers Jr., M.G.1    Mendez, R.2    Shi, P.3    Pierce, J.H.4    Rhoads, R.5    White, M.F.6
  • 19
    • 0034282455 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of paxillin alpha is involved in temporospatial regulation of paxillin-containing focal adhesion formation and F-actin organization in motile cells
    • Nakamura K, Yano H, Uchida H, Hashimoto S, Schaefer E, Sabe H. 2000. Tyrosine phosphorylation of paxillin alpha is involved in temporospatial regulation of paxillin-containing focal adhesion formation and F-actin organization in motile cells. J Biol Chem 275(35):27155-27164.
    • (2000) J Biol Chem , vol.275 , Issue.35 , pp. 27155-27164
    • Nakamura, K.1    Yano, H.2    Uchida, H.3    Hashimoto, S.4    Schaefer, E.5    Sabe, H.6
  • 20
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes CD, Hall A. 1995. Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81(1):53-62.
    • (1995) Cell , vol.81 , Issue.1 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 21
    • 0033538615 scopus 로고    scopus 로고
    • Mechanotransduction of rat aortic vascular smooth muscle cells requires RhoA and intact actin filaments
    • Numaguchi K, Eguchi S, Yamakawa T, Motley ED, Inagami T. 1999. Mechanotransduction of rat aortic vascular smooth muscle cells requires RhoA and intact actin filaments. Circ Res 85(1):5-11.
    • (1999) Circ Res , vol.85 , Issue.1 , pp. 5-11
    • Numaguchi, K.1    Eguchi, S.2    Yamakawa, T.3    Motley, E.D.4    Inagami, T.5
  • 22
    • 0036357414 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of paxillin, FAK, and p130CAS: Effects on cell spreading and migration
    • Panetti TS. 2002. Tyrosine phosphorylation of paxillin, FAK, and p130CAS: Effects on cell spreading and migration. Front Biosci 7:d143-d150.
    • (2002) Front Biosci , vol.7
    • Panetti, T.S.1
  • 23
    • 0033081753 scopus 로고    scopus 로고
    • Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton
    • Ren XD, Kiosses WB, Schwartz MA. 1999. Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. Embo J 18(3):578-585.
    • (1999) Embo J , vol.18 , Issue.3 , pp. 578-585
    • Ren, X.D.1    Kiosses, W.B.2    Schwartz, M.A.3
  • 24
  • 26
    • 0032577738 scopus 로고    scopus 로고
    • Phosphorylation of p130Cas by angiotensin II is dependent on c-Src, intracellular Ca2+, and protein kinase C
    • Sayeski PP, Ali MS, Harp JB, Marrero MB, Bernstein KE. 1998. Phosphorylation of p130Cas by angiotensin II is dependent on c-Src, intracellular Ca2+, and protein kinase C. Circ Res 82(12):1279-1288.
    • (1998) Circ Res , vol.82 , Issue.12 , pp. 1279-1288
    • Sayeski, P.P.1    Ali, M.S.2    Harp, J.B.3    Marrero, M.B.4    Bernstein, K.E.5
  • 28
    • 0036644975 scopus 로고    scopus 로고
    • Guanine nucleotide exchange factors for Rho GTPases: Turning on the switch
    • Schmidt A, Hall A. 2002. Guanine nucleotide exchange factors for Rho GTPases: Turning on the switch. Genes Dev 16(13):1587-1609.
    • (2002) Genes Dev , vol.16 , Issue.13 , pp. 1587-1609
    • Schmidt, A.1    Hall, A.2
  • 29
    • 0035933742 scopus 로고    scopus 로고
    • Angiotensin II-induced stimulation of p21-activated kinase and c-Jun NH2-terminal kinase is mediated by Rac1 and Nck
    • Schmitz U, Thommes K, Beier I, Wagner W, Sachinidis A, Dusing R, Vetter H. 2001. Angiotensin II-induced stimulation of p21-activated kinase and c-Jun NH2-terminal kinase is mediated by Rac1 and Nck. J Biol Chem 276 (25):22003-22010.
    • (2001) J Biol Chem , vol.276 , Issue.25 , pp. 22003-22010
    • Schmitz, U.1    Thommes, K.2    Beier, I.3    Wagner, W.4    Sachinidis, A.5    Dusing, R.6    Vetter, H.7
  • 31
    • 0032513047 scopus 로고    scopus 로고
    • Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin
    • Shen Y, Schneider G, Cloutier JF, Veillette A, Schaller MD. 1998. Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin. J Biol Chem 273(11):6474-6481.
    • (1998) J Biol Chem , vol.273 , Issue.11 , pp. 6474-6481
    • Shen, Y.1    Schneider, G.2    Cloutier, J.F.3    Veillette, A.4    Schaller, M.D.5
  • 32
    • 0036080671 scopus 로고    scopus 로고
    • Altered regulation of SHP-2 and PTP 1B tyrosine phosphatases in cystic kidneys from bcl-2 -/- Mice
    • Sorenson CM, Sheibani N. 2002. Altered regulation of SHP-2 and PTP 1B tyrosine phosphatases in cystic kidneys from bcl-2 -/- mice. Am J Physiol Renal Physiol 282(3):F442-450.
    • (2002) Am J Physiol Renal Physiol , vol.282 , Issue.3
    • Sorenson, C.M.1    Sheibani, N.2
  • 33
    • 0032486198 scopus 로고    scopus 로고
    • Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN
    • Tamura M, Gu J, Matsumoto K, Aota S, Parsons R, Yamada KM. 1998. Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN. Science 280(5369):1614-1617.
    • (1998) Science , vol.280 , Issue.5369 , pp. 1614-1617
    • Tamura, M.1    Gu, J.2    Matsumoto, K.3    Aota, S.4    Parsons, R.5    Yamada, K.M.6
  • 34
    • 0035877754 scopus 로고    scopus 로고
    • Vav2 activates c-fos serum response element and CD69 expression but negatively regulates nuclear factor of activated T cells and interleukin-2 gene activation in T lymphocyte
    • Tartare-Deckert S, Monthouel MN, Charvet C, Foucault I, Van Obberghen E, Bernard A, Altman A, Deckert M. 2001. Vav2 activates c-fos serum response element and CD69 expression but negatively regulates nuclear factor of activated T cells and interleukin-2 gene activation in T lymphocyte. J Biol Chem 276(24):20849-20857.
    • (2001) J Biol Chem , vol.276 , Issue.24 , pp. 20849-20857
    • Tartare-Deckert, S.1    Monthouel, M.N.2    Charvet, C.3    Foucault, I.4    Van Obberghen, E.5    Bernard, A.6    Altman, A.7    Deckert, M.8
  • 35
    • 0027254306 scopus 로고
    • Tyrosine phosphorylation of the focal adhesion kinase pp125FAK during development: Relation to paxillin
    • Turner CE, Schaller MD, Parsons JT. 1993. Tyrosine phosphorylation of the focal adhesion kinase pp125FAK during development: Relation to paxillin. J Cell Sci 105(Pt 3):637-645.
    • (1993) J Cell Sci , vol.105 , Issue.PART 3 , pp. 637-645
    • Turner, C.E.1    Schaller, M.D.2    Parsons, J.T.3
  • 36
    • 0028802024 scopus 로고
    • Angiotensin II stimulation of rapid paxillin tyrosine phosphorylation correlates with the formation of focal adhesions in rat aortic smooth muscle cells
    • Turner CE, Pietras KM, Taylor DS, Molloy CJ. 1995. Angiotensin II stimulation of rapid paxillin tyrosine phosphorylation correlates with the formation of focal adhesions in rat aortic smooth muscle cells. J Cell Sci 108(Pt 1):333-342.
    • (1995) J Cell Sci , vol.108 , Issue.PART 1 , pp. 333-342
    • Turner, C.E.1    Pietras, K.M.2    Taylor, D.S.3    Molloy, C.J.4
  • 37
    • 0036135726 scopus 로고    scopus 로고
    • Differential regulation of components of the focal adhesion complex by heregulin: Role of phosphatase SHP-2
    • Vadlamudi RK, Adam L, Nguyen D, Santos M, Kumar R. 2002. Differential regulation of components of the focal adhesion complex by heregulin: Role of phosphatase SHP-2. J Cell Physiol 190(2):189-199.
    • (2002) J Cell Physiol , vol.190 , Issue.2 , pp. 189-199
    • Vadlamudi, R.K.1    Adam, L.2    Nguyen, D.3    Santos, M.4    Kumar, R.5
  • 38
    • 0036156348 scopus 로고    scopus 로고
    • Molecular interactions of SHP1 and SHP2 in IL-3-signalling
    • Wheadon H, Paling NR, Welham MJ. 2002. Molecular interactions of SHP1 and SHP2 in IL-3-signalling. Cell Signal 14(3):219-229.
    • (2002) Cell Signal , vol.14 , Issue.3 , pp. 219-229
    • Wheadon, H.1    Paling, N.R.2    Welham, M.J.3
  • 40
    • 0035800750 scopus 로고    scopus 로고
    • Association of tyrosine phosphatase SHP-2 with F-actin at low cell densities
    • Xu F, Zhao R, Peng Y, Guerrah A, Zhao ZJ. 2001. Association of tyrosine phosphatase SHP-2 with F-actin at low cell densities. J Biol Chem 276(31):29479-29484.
    • (2001) J Biol Chem , vol.276 , Issue.31 , pp. 29479-29484
    • Xu, F.1    Zhao, R.2    Peng, Y.3    Guerrah, A.4    Zhao, Z.J.5
  • 41
    • 3543036342 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion
    • Yu DH, Qu CK, Henegariu O, Lu X, Feng GS. 1998. Protein-tyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion. J Biol Chem 273(33):21125-21131.
    • (1998) J Biol Chem , vol.273 , Issue.33 , pp. 21125-21131
    • Yu, D.H.1    Qu, C.K.2    Henegariu, O.3    Lu, X.4    Feng, G.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.