메뉴 건너뛰기




Volumn 7, Issue 3, 1996, Pages 415-423

Tyrosine Phosphorylation of Focal Adhesion Kinase (p125FAK): Regulation by cAMP and Thrombin in Mesangial Cells

Author keywords

Cell shape; Focal adhesion kinase; Mesangial cell

Indexed keywords

CYCLIC AMP; CYTOCHALASIN D; FOCAL ADHESION KINASE; NOCODAZOLE; THROMBIN; TYROSINE;

EID: 0029960996     PISSN: 10466673     EISSN: None     Source Type: Journal    
DOI: 10.1681/asn.v73415     Document Type: Article
Times cited : (18)

References (54)
  • 1
    • 0023684353 scopus 로고
    • Regulation of thrombin generation and functions
    • Fenton JW: Regulation of thrombin generation and functions. Semin Thromb Hemostasis 1988;14:234-240.
    • (1988) Semin Thromb Hemostasis , vol.14 , pp. 234-240
    • Fenton, J.W.1
  • 2
    • 0024385050 scopus 로고
    • Mitogenic signals for thrombin in mesangial cells: Regulation of phospholipase C and PDGF genes
    • Shultz PJ, Knauss TC, Mene P, Abboud H: Mitogenic signals for thrombin in mesangial cells: Regulation of phospholipase C and PDGF genes. Am J Physiol 1989; 257:F366-F374.
    • (1989) Am J Physiol , vol.257
    • Shultz, P.J.1    Knauss, T.C.2    Mene, P.3    Abboud, H.4
  • 4
    • 0025732353 scopus 로고
    • Expression of smooth muscle cell phenotype by rat mesangial cells in immune complex nephritis
    • Johnson RJ, Iida H, Alpers CE. et al.: Expression of smooth muscle cell phenotype by rat mesangial cells in immune complex nephritis. J Clin Invest 1991;87:847-858.
    • (1991) J Clin Invest , vol.87 , pp. 847-858
    • Johnson, R.J.1    Iida, H.2    Alpers, C.E.3
  • 7
    • 0021249263 scopus 로고
    • The composition of glomerulosclerosis. I. Studies in focal sclerosis, crescentic glomerulonephritis, and membranoproliferative glomerulonephritis
    • Striker LM, Killen PD, Chi E, Striker GE: The composition of glomerulosclerosis. I. Studies in focal sclerosis, crescentic glomerulonephritis, and membranoproliferative glomerulonephritis. Lab Invest 1984;51:181-192
    • (1984) Lab Invest , vol.51 , pp. 181-192
    • Striker, L.M.1    Killen, P.D.2    Chi, E.3    Striker, G.E.4
  • 9
    • 0026742944 scopus 로고
    • Cell-matrix adhesion receptors: Relevance to glomerular pathology
    • Cosio F: Cell-matrix adhesion receptors: Relevance to glomerular pathology. Am J Kidney Dis 1992;20:294-305.
    • (1992) Am J Kidney Dis , vol.20 , pp. 294-305
    • Cosio, F.1
  • 10
    • 0027291705 scopus 로고
    • Focal adhesion kinase: An integrin-linked protein tyrosine kinase
    • Schaller MD, Parsons JT: Focal adhesion kinase: An integrin-linked protein tyrosine kinase. Trends in Cell Biol 1993;3:258-262.
    • (1993) Trends in Cell Biol , vol.3 , pp. 258-262
    • Schaller, M.D.1    Parsons, J.T.2
  • 11
    • 0027055575 scopus 로고
    • Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase
    • Kornberg L, Earp HS, Parsons JT, Schaller M, Juliano RL: Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase. J Biol Chem 1992;267:23439-23442.
    • (1992) J Biol Chem , vol.267 , pp. 23439-23442
    • Kornberg, L.1    Earp, H.S.2    Parsons, J.T.3    Schaller, M.4    Juliano, R.L.5
  • 12
    • 0025745212 scopus 로고
    • Insoluble fibronectin activates the Na/H antiporter by clustering and immobilizing integrin α5β1, independent of cell shape
    • Schwartz MA, Lechene C, Ingber DE: Insoluble fibronectin activates the Na/H antiporter by clustering and immobilizing integrin α5β1, independent of cell shape. Proc Natl Acad Sci USA 1991;88:7849-7853.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7849-7853
    • Schwartz, M.A.1    Lechene, C.2    Ingber, D.E.3
  • 13
    • 0027176804 scopus 로고
    • Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown
    • McNamee HP, Ingber DE, Schwartz MA: Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown. J Cell Biol 1993;121:673-678.
    • (1993) J Cell Biol , vol.121 , pp. 673-678
    • McNamee, H.P.1    Ingber, D.E.2    Schwartz, M.A.3
  • 15
    • 0026700191 scopus 로고
    • Bombesin, vasopressin, and endothelin stimulation of tyrosine phosphorylation in Swiss 3T3 cells. Identification of a novel tyrosine kinase as a major substrate
    • Zachary I, Sinnett-Smith J, Rozengurt E: Bombesin, vasopressin, and endothelin stimulation of tyrosine phosphorylation in Swiss 3T3 cells. Identification of a novel tyrosine kinase as a major substrate. J Biol Chem 1992;267:19031-19034.
    • (1992) J Biol Chem , vol.267 , pp. 19031-19034
    • Zachary, I.1    Sinnett-Smith, J.2    Rozengurt, E.3
  • 16
    • 0025376378 scopus 로고
    • Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases
    • Kanner SB, Reynolds AB, Vines RR, Parsons JT: Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases. Proc Natl Acad Sci USA 1990;87:3328-3332.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3328-3332
    • Kanner, S.B.1    Reynolds, A.B.2    Vines, R.R.3    Parsons, J.T.4
  • 17
    • 0028109766 scopus 로고
    • Regulation of protein tyrosine kinases in platelets
    • Clark E, Shattil SJ, Brugge JS: Regulation of protein tyrosine kinases in platelets. Trends Biochem Sci 1994; 19:464-469.
    • (1994) Trends Biochem Sci , vol.19 , pp. 464-469
    • Clark, E.1    Shattil, S.J.2    Brugge, J.S.3
  • 18
  • 19
    • 0026699905 scopus 로고
    • Stimulation of the thrombin receptor of human glomerular mesangial cells by Ser-Phe-Leu-Arg-Asn-Pro-Asn-Asp-Lys-Tyr-Glu-Pro-Phe peptide
    • Troyer D, Padilla R, Smith T, Kreisberg J, Glass W: Stimulation of the thrombin receptor of human glomerular mesangial cells by Ser-Phe-Leu-Arg-Asn-Pro-Asn-Asp-Lys-Tyr-Glu-Pro-Phe peptide. J Biol Chem 1992; 267:20126-20131.
    • (1992) J Biol Chem , vol.267 , pp. 20126-20131
    • Troyer, D.1    Padilla, R.2    Smith, T.3    Kreisberg, J.4    Glass, W.5
  • 20
    • 0015009307 scopus 로고
    • Morphological transformation of Chinese hamster cells by dibutyryl adenosine cyclic 3′:5″-monophosphate and testosterone
    • Hsie AW, Puck TT: Morphological transformation Of Chinese hamster cells by dibutyryl adenosine cyclic 3′:5″-monophosphate and testosterone. Proc Natl Acad Sci USA 1971;68:358-361.
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 358-361
    • Hsie, A.W.1    Puck, T.T.2
  • 21
    • 3042862469 scopus 로고
    • Induction of the stellate configuration in cultured iris epithelial cells by adenosine and compounds related to adenosine 3′:5′-cyclic monophosphate
    • Ortiz JR, Yamada T, Hsie AW: Induction of the stellate configuration in cultured iris epithelial cells by adenosine and compounds related to adenosine 3′:5′-cyclic monophosphate. Proc Natl Acad Sci USA 1973;70:2286-2290.
    • (1973) Proc Natl Acad Sci USA , vol.70 , pp. 2286-2290
    • Ortiz, J.R.1    Yamada, T.2    Hsie, A.W.3
  • 22
    • 0019042735 scopus 로고
    • Electron microscopic immunocyto-chemical localization of intracellular antigens in cultured cells: The EGS and ferritin bridge procedures
    • Willingham MC: Electron microscopic immunocyto-chemical localization of intracellular antigens in cultured cells: The EGS and ferritin bridge procedures. Histochem J 1980;12:419-434.
    • (1980) Histochem J , vol.12 , pp. 419-434
    • Willingham, M.C.1
  • 23
    • 0027190844 scopus 로고
    • Mechanisms for actin reorganization in chemotactic factor activated polymorphonuclear leukocytes
    • Watts RG, Howard TH: Mechanisms for actin reorganization in chemotactic factor activated polymorphonuclear leukocytes. Blood 1993;81:2750-2757.
    • (1993) Blood , vol.81 , pp. 2750-2757
    • Watts, R.G.1    Howard, T.H.2
  • 24
    • 0022555884 scopus 로고
    • Actin and actin binding proteins. A critical evaluation of mechanisms and functions
    • Pollard TD, Cooper JA: Actin and actin binding proteins. A critical evaluation of mechanisms and functions. Annu Rev Biochem 1986;55:987-1035.
    • (1986) Annu Rev Biochem , vol.55 , pp. 987-1035
    • Pollard, T.D.1    Cooper, J.A.2
  • 25
    • 0027470173 scopus 로고
    • Two-chain urokinase, receptor, and type 1 inhibitor in cultured human mesangial cells
    • Glass WF, Kreisberg JI, Troyer DA: Two-chain urokinase, receptor, and type 1 inhibitor in cultured human mesangial cells. Am J Physiol 1993;264:F532-F539.
    • (1993) Am J Physiol , vol.264
    • Glass, W.F.1    Kreisberg, J.I.2    Troyer, D.A.3
  • 26
    • 0017691683 scopus 로고
    • Correlation between changes in intracellular level of cyclic AMP, activation of cyclic AMP-dependent protein kinase, and the morphology of Chines hamster ovary cells in culture
    • Li AP, O'Neill P, Kawashima K, Hsie AW: Correlation between changes in intracellular level of cyclic AMP, activation of cyclic AMP-dependent protein kinase, and the morphology of Chines hamster ovary cells in culture. Arch Biochem Biophys 1977;182:181-187.
    • (1977) Arch Biochem Biophys , vol.182 , pp. 181-187
    • Li, A.P.1    O'Neill, P.2    Kawashima, K.3    Hsie, A.W.4
  • 27
    • 0027508511 scopus 로고
    • Regulation of integrin-mediated adhesion at focal contacts by cyclic AMP
    • Glass WF, Kreisberg JI: Regulation of integrin-mediated adhesion at focal contacts by cyclic AMP. J Cellular Physiol 1993;157:296-306.
    • (1993) J Cellular Physiol , vol.157 , pp. 296-306
    • Glass, W.F.1    Kreisberg, J.I.2
  • 28
    • 0023031861 scopus 로고
    • Vasoactive agents affect mesangial cell adhesion
    • Kreisberg JI, Venkatachalam MA: Vasoactive agents affect mesangial cell adhesion. Am J Physiol 1986;251: C505-C511.
    • (1986) Am J Physiol , vol.251
    • Kreisberg, J.I.1    Venkatachalam, M.A.2
  • 29
    • 0022106730 scopus 로고
    • Role of myosin light-chain phosphorylation and microtubules in stress fiber morphology in cultured mesangial cells
    • Kreisberg JI, Venkatachalam MA, Radnik RA, Patel PY: Role of myosin light-chain phosphorylation and microtubules in stress fiber morphology in cultured mesangial cells. Am J Physiol 1985;249:F227-F235.
    • (1985) Am J Physiol , vol.249
    • Kreisberg, J.I.1    Venkatachalam, M.A.2    Radnik, R.A.3    Patel, P.Y.4
  • 30
    • 0025982039 scopus 로고
    • The role of actin polymerization in cell motility
    • Cooper JA: The role of actin polymerization in cell motility. Annu Rev Physiol 1991;53:585-605.
    • (1991) Annu Rev Physiol , vol.53 , pp. 585-605
    • Cooper, J.A.1
  • 31
    • 0026035523 scopus 로고
    • Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
    • Vu TK, Hung DT, Wheaton VI, Coughlin SR: Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell 1991; 64:1057-1068.
    • (1991) Cell , vol.64 , pp. 1057-1068
    • Vu, T.K.1    Hung, D.T.2    Wheaton, V.I.3    Coughlin, S.R.4
  • 33
    • 0026756594 scopus 로고
    • Requirement of phosphatidylinositol 4,5-bisphosphate for a-actinin function
    • Fukami K, Furuhashi K, Inagaki M, Endo T, Hatano S, Takenawa T: Requirement of phosphatidylinositol 4,5-bisphosphate for a-actinin function. Nature 1989;359: 150-152.
    • (1989) Nature , vol.359 , pp. 150-152
    • Fukami, K.1    Furuhashi, K.2    Inagaki, M.3    Endo, T.4    Hatano, S.5    Takenawa, T.6
  • 34
    • 0021919105 scopus 로고
    • Specific interaction between phosphatidylinositol-4,5-bisphosphate and profilactin
    • Lassing I, Lindberg U: Specific interaction between phosphatidylinositol-4,5-bisphosphate and profilactin. Nature 1985;314:472-474.
    • (1985) Nature , vol.314 , pp. 472-474
    • Lassing, I.1    Lindberg, U.2
  • 35
    • 85190681974 scopus 로고
    • Inositol lipids dissociate gelsolin-actin complexes
    • Janmey PA, Ada KI, Yin HL, Stossel TP: Inositol lipids dissociate gelsolin-actin complexes. J Biol Chem 1987; 262:12228-12236.
    • (1987) J Biol Chem , vol.262 , pp. 12228-12236
    • Janmey, P.A.1    Ada, K.I.2    Yin, H.L.3    Stossel, T.P.4
  • 36
    • 0025651999 scopus 로고
    • Cap39, a calcium ion- and polyphosphoinositide-regulated actin capping protein
    • Washington DC
    • Yu FX, Johnston PA, Sudhof TC, Yin HL: Cap39, a calcium ion-and polyphosphoinositide-regulated actin capping protein. Science (Washington DC) 1990;250: 1413-1415.
    • (1990) Science , vol.250 , pp. 1413-1415
    • Yu, F.X.1    Johnston, P.A.2    Sudhof, T.C.3    Yin, H.L.4
  • 37
    • 0027176804 scopus 로고
    • Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown
    • McNamee HP, Ingber DE, Schwartz MA: Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown. J Cell Biol 1993;121:673-678.
    • (1993) J Cell Biol , vol.121 , pp. 673-678
    • McNamee, H.P.1    Ingber, D.E.2    Schwartz, M.A.3
  • 38
    • 0028036684 scopus 로고
    • The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • Chong LD, Traynor-Kaplan A, Bokoch GM, Schwartz MA: The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 1994;79:507-513.
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.D.1    Traynor-Kaplan, A.2    Bokoch, G.M.3    Schwartz, M.A.4
  • 39
    • 0028174102 scopus 로고
    • α-actinin and vinculin are PIP2-binding proteins involved in signaling by tyrosine kinase
    • Fukami K, Endo T, Imamura M, Takenawa T: α-actinin and vinculin are PIP2-binding proteins involved in signaling by tyrosine kinase. J Biol Chem 1994;269:1518-1522.
    • (1994) J Biol Chem , vol.269 , pp. 1518-1522
    • Fukami, K.1    Endo, T.2    Imamura, M.3    Takenawa, T.4
  • 40
    • 0026774568 scopus 로고
    • Activated phosphoinositide 3-kinase associates with membrane skeleton in thrombin-exposed plateletes
    • Zhang J, Fry MJ, Waterfield MD, et al.: Activated phosphoinositide 3-kinase associates with membrane skeleton in thrombin-exposed plateletes. J Biol Chem 1992; 267:4686-4692.
    • (1992) J Biol Chem , vol.267 , pp. 4686-4692
    • Zhang, J.1    Fry, M.J.2    Waterfield, M.D.3
  • 41
    • 0024567044 scopus 로고
    • Gelsolin-polyphosphoinositide interaction
    • Janmey PA, Stossel TP: Gelsolin-polyphosphoinositide interaction. J Biol Chem 1989;264:4825-4831.
    • (1989) J Biol Chem , vol.264 , pp. 4825-4831
    • Janmey, P.A.1    Stossel, T.P.2
  • 42
    • 0027299745 scopus 로고
    • On the crawling of animal cells
    • Washington DC
    • Stossel TP: On the crawling of animal cells. Science (Washington DC) 1993;260:1086-1094.
    • (1993) Science , vol.260 , pp. 1086-1094
    • Stossel, T.P.1
  • 43
    • 85190664594 scopus 로고
    • Fibroblast stress-relaxation activates a cyclic AMP signaling pathway
    • He J, Grinnell F: Fibroblast stress-relaxation activates a cyclic AMP signaling pathway [Abstract]. Mol Biol Cell 1993;4:364A.
    • (1993) Mol Biol Cell , vol.4
    • He, J.1    Grinnell, F.2
  • 44
    • 0023695794 scopus 로고
    • Regulation of actin microfilament integrity in living nonmuscle cells by the cAMP-dependent protein kinase and the myosin light chain kinase
    • Lamb NJC, Fernandez A, Conti MA, et al.: Regulation of actin microfilament integrity in living nonmuscle cells by the cAMP-dependent protein kinase and the myosin light chain kinase. J Cell Biol 1988;106:1955-1971.
    • (1988) J Cell Biol , vol.106 , pp. 1955-1971
    • Lamb, N.J.C.1    Fernandez, A.2    Conti, M.A.3
  • 45
    • 0025363197 scopus 로고
    • Protein phosphatase type-1, not type-2A, modulates actin microfilament integrity and myosin light chain phosphorylation in living nonmuscle cells
    • Fernandez A, Brautigan DL, Mumby M, Lamb JJC: Protein phosphatase type-1, not type-2A, modulates actin microfilament integrity and myosin light chain phosphorylation in living nonmuscle cells. J Cell Biol 1990; 111:103-112.
    • (1990) J Cell Biol , vol.111 , pp. 103-112
    • Fernandez, A.1    Brautigan, D.L.2    Mumby, M.3    Lamb, J.J.C.4
  • 46
    • 84941139842 scopus 로고
    • Localization of myosin light chain kinase in non-muscle cells
    • Rosen OA, Drebs EG, Eds. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Feramisco JR, Burridge K deLanerolle P, Adelstein RS. Localization of myosin light chain kinase in non-muscle cells. In: Rosen OA, Drebs EG, Eds. Protein Phosphorylation. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press; 1982:855-868.
    • (1982) Protein Phosphorylation , pp. 855-868
    • Feramisco, J.R.1    Burridge, K.2    DeLanerolle, P.3    Adelstein, R.S.4
  • 47
    • 0002332210 scopus 로고    scopus 로고
    • Tension and compression as basic determinants of cell form and function: Utilization of a tensegrity mechanism
    • Stein WD, Bronner F, Eds. Cell Shape: Academic Press
    • Ingber DE, Folkman J. Tension and compression as basic determinants of cell form and function: Utilization of a tensegrity mechanism. In: Stein WD, Bronner F, Eds. Cell Shape: Determinants, Regulation, and Regulatory Role. Academic Press, pp. 3-31.
    • Determinants, Regulation, and Regulatory Role , pp. 3-31
    • Ingber, D.E.1    Folkman, J.2
  • 48
    • 0026643589 scopus 로고
    • Effects of vinblastine, podophyllotoxin and nocodazole on mitotic spindles
    • Jordan MA, Thrower D, Wilson L: Effects of vinblastine, podophyllotoxin and nocodazole on mitotic spindles. J Cell Sci 1992;102:401-416.
    • (1992) J Cell Sci , vol.102 , pp. 401-416
    • Jordan, M.A.1    Thrower, D.2    Wilson, L.3
  • 49
    • 0024325593 scopus 로고
    • Fibroblast contractility and actin organization are sitmulated by microtubule inhibitors
    • Danowski BA: Fibroblast contractility and actin organization are sitmulated by microtubule inhibitors. J Cell Sci 1989;93:255-266.
    • (1989) J Cell Sci , vol.93 , pp. 255-266
    • Danowski, B.A.1
  • 50
    • 0024553897 scopus 로고
    • Binding of kinesin to stress fibers in fibroblasts under conditions of microtubule depolymerization
    • Okuhara K, Murofushi H, Sakai H: Binding of kinesin to stress fibers in fibroblasts under conditions of microtubule depolymerization. Cell Motil Cytoskeleton 1989;12: 71-77.
    • (1989) Cell Motil Cytoskeleton , vol.12 , pp. 71-77
    • Okuhara, K.1    Murofushi, H.2    Sakai, H.3
  • 51
    • 0027153594 scopus 로고
    • Bombesin stimulation of p125 focal adhesion kinase tyrosine phosphorylation
    • Sinnett-Smith J, Zachary, Valverde AM, Rozengurt E: Bombesin stimulation of p125 focal adhesion kinase tyrosine phosphorylation. J Biol Chem 1993;268: 14261-14268.
    • (1993) J Biol Chem , vol.268 , pp. 14261-14268
    • Sinnett-Smith, J.1    Zachary2    Valverde, A.M.3    Rozengurt, E.4
  • 52
    • 0027221483 scopus 로고
    • Cellular tensegrity: Defining new rules of biological design that govern the cytoskeleton
    • Ingber DE: Cellular tensegrity: Defining new rules of biological design that govern the cytoskeleton. J Cell Sci 1993;104:613-627.
    • (1993) J Cell Sci , vol.104 , pp. 613-627
    • Ingber, D.E.1
  • 53
    • 0026578878 scopus 로고
    • Mechanical forces and their second messengers in stimulating cell growth in vitro
    • Vandenburgh HH: Mechanical forces and their second messengers in stimulating cell growth in vitro. Am J Physiol 1992;262:R350-R355.
    • (1992) Am J Physiol , vol.262
    • Vandenburgh, H.H.1
  • 54
    • 0027196279 scopus 로고
    • Cytoskeletal role in contractile dysfunction of hypertrophied myocardium
    • Washington DC
    • Tsutsui H, Ishihasa K, Cooper G: Cytoskeletal role in contractile dysfunction of hypertrophied myocardium. Science (Washington DC) 1993;260:682-687.
    • (1993) Science , vol.260 , pp. 682-687
    • Tsutsui, H.1    Ishihasa, K.2    Cooper, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.