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Volumn 408, Issue 1, 2007, Pages 7-18

Targeting of FAK Ser910 by ERK5 and PP1δ in non-stimulated and phorbol ester-stimulated cells

Author keywords

Cell motility; Cell survival; Extracellular signal regulated kinase 5 (ERK5); Focal adhesion kinase (FAK); Phorbol ester; Protein phosphatase 1 (PP1)

Indexed keywords

CELL DEATH; ENZYME ACTIVITY; ENZYME INHIBITION; PHOSPHORYLATION;

EID: 36349020785     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070058     Document Type: Article
Times cited : (18)

References (37)
  • 1
    • 0142141199 scopus 로고    scopus 로고
    • Focal adhesion kinase signaling activities and their implications in the control of cell survival and motility
    • Hanks, S. K., Ryzhova, L., Shin, N. and Brabek, J. (2003) Focal adhesion kinase signaling activities and their implications in the control of cell survival and motility. Front. Biosci. 8, d982-d986
    • (2003) Front. Biosci , vol.8
    • Hanks, S.K.1    Ryzhova, L.2    Shin, N.3    Brabek, J.4
  • 2
    • 0037509990 scopus 로고    scopus 로고
    • Focal adhesion kinase: The first ten years
    • Parsons, J. T. (2003) Focal adhesion kinase: the first ten years. J. Cell Sci. 116, 1409-1416
    • (2003) J. Cell Sci , vol.116 , pp. 1409-1416
    • Parsons, J.T.1
  • 3
    • 2342472716 scopus 로고    scopus 로고
    • Focal adhesion and actin dynamics: A place where kinases and proteases meet to promote invasion
    • Carragher, N. O. and Frame, M. C. (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
  • 4
    • 0033002997 scopus 로고    scopus 로고
    • Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2
    • Owen, J. D., Ruest, P. J., Fry, D. W. and Hanks, S. K. (1999) Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2. Mol. Cell. Biol. 19, 4806-4818
    • (1999) Mol. Cell. Biol , vol.19 , pp. 4806-4818
    • Owen, J.D.1    Ruest, P.J.2    Fry, D.W.3    Hanks, S.K.4
  • 5
    • 3142521875 scopus 로고    scopus 로고
    • Control of motile and invasive phenotypes by focal adhesion kinase
    • Schlaepfer, D. D., Mitra, S. K. and Ilic, D. (2004) Control of motile and invasive phenotypes by focal adhesion kinase. Biochim. Biophys. Acta 1692, 77-102
    • (2004) Biochim. Biophys. Acta , vol.1692 , pp. 77-102
    • Schlaepfer, D.D.1    Mitra, S.K.2    Ilic, D.3
  • 7
    • 33748286819 scopus 로고    scopus 로고
    • Integrin-regulated FAK-Src signaling in normal and cancer cells
    • Mitra, S. K. and Schlaepfer, D. D. (2006) Integrin-regulated FAK-Src signaling in normal and cancer cells. Curr. Opin. Cell Biol. 18, 516-523
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 516-523
    • Mitra, S.K.1    Schlaepfer, D.D.2
  • 11
    • 3042776220 scopus 로고    scopus 로고
    • PDGF and FGF induce focal adhesion kinase (FAK) phosphorylation at Ser-910: Dissociation from Tyr-397 phosphorylation and requirement for ERK activation
    • Hunger-Glaser, I., Fan, R. S., Perez-Salazar, E. and Rozengurt, E. (2004) PDGF and FGF induce focal adhesion kinase (FAK) phosphorylation at Ser-910: dissociation from Tyr-397 phosphorylation and requirement for ERK activation. J. Cell. Physiol. 200, 213-222
    • (2004) J. Cell. Physiol , vol.200 , pp. 213-222
    • Hunger-Glaser, I.1    Fan, R.S.2    Perez-Salazar, E.3    Rozengurt, E.4
  • 12
    • 0037927994 scopus 로고    scopus 로고
    • Bombesin, lysophosphatidic acid, and epidermal growth factor rapidly stimulate focal adhesion kinase phosphorylation at Ser-910
    • Hunger-Glaser, l., Perez-Salazar, E., Sinnett-Smith, J. and Rozengurt, E. (2003) Bombesin, lysophosphatidic acid, and epidermal growth factor rapidly stimulate focal adhesion kinase phosphorylation at Ser-910. J. Biol. Chem. 278, 22631-22643
    • (2003) J. Biol. Chem , vol.278 , pp. 22631-22643
    • Hunger-Glaser, L.1    Perez-Salazar, E.2    Sinnett-Smith, J.3    Rozengurt, E.4
  • 13
    • 0030917676 scopus 로고    scopus 로고
    • Identification of integrin-stimulated sites of serine phosphorylation in FRNK, the separately expressed C-terminal domain of focal adhesion kinase: A potential role for protein kinase A
    • Richardson, A., Shannon, J. D., Adams, R. B., Schaller, M. D. and Parsons, J. T. (1997) Identification of integrin-stimulated sites of serine phosphorylation in FRNK, the separately expressed C-terminal domain of focal adhesion kinase: a potential role for protein kinase A. Biochem. J. 324, 141-149
    • (1997) Biochem. J , vol.324 , pp. 141-149
    • Richardson, A.1    Shannon, J.D.2    Adams, R.B.3    Schaller, M.D.4    Parsons, J.T.5
  • 14
    • 4644328892 scopus 로고    scopus 로고
    • Paxillin: Adapting to change
    • Brown, M. C. and Turner, C. E. (2004) Paxillin: adapting to change. Physiol. Rev. 84, 1315-1339
    • (2004) Physiol. Rev , vol.84 , pp. 1315-1339
    • Brown, M.C.1    Turner, C.E.2
  • 15
    • 0033601745 scopus 로고    scopus 로고
    • Dissociation of FAK/p130(CAS)/c-Src complexes during mitosis: Role of mitosis-specific serine phosphorylation of FAK
    • Yamakita, Y., Totsukawa, G., Yamashiro, S., Fry, D., Zhang, X., Hanks, S. K. and Matsumura, F. (1999) Dissociation of FAK/p130(CAS)/c-Src complexes during mitosis: role of mitosis-specific serine phosphorylation of FAK. J. Cell Biol. 144, 315-324
    • (1999) J. Cell Biol , vol.144 , pp. 315-324
    • Yamakita, Y.1    Totsukawa, G.2    Yamashiro, S.3    Fry, D.4    Zhang, X.5    Hanks, S.K.6    Matsumura, F.7
  • 16
    • 0035447707 scopus 로고    scopus 로고
    • Cell-cycle-dependent association of protein phosphatase 1 and focal adhesion kinase
    • Fresu, M., Bianchi, M., Parsons, J. T. and Villa-Moruzzi, E. (2001) Cell-cycle-dependent association of protein phosphatase 1 and focal adhesion kinase. Biochem. J. 350, 407-414
    • (2001) Biochem. J , vol.350 , pp. 407-414
    • Fresu, M.1    Bianchi, M.2    Parsons, J.T.3    Villa-Moruzzi, E.4
  • 17
    • 0346728803 scopus 로고    scopus 로고
    • Functional diversity of protein phosphatase-1, a cellular economizer and reset button
    • Ceulemans, H. and Bollen, M. (2004) Functional diversity of protein phosphatase-1, a cellular economizer and reset button. Physiol. Rev. 84, 1-39
    • (2004) Physiol. Rev , vol.84 , pp. 1-39
    • Ceulemans, H.1    Bollen, M.2
  • 18
    • 0031004803 scopus 로고    scopus 로고
    • Differential localization of myosin and myosin phosphatase subunits in smooth muscle cells and migrating fibroblasts
    • Murata, K., Hirano, K., Villa-Moruzzi, E., Hartshorne, D. J. and Brautigan, D. L. (1997) Differential localization of myosin and myosin phosphatase subunits in smooth muscle cells and migrating fibroblasts. Mol. Biol. Cell 8, 663-673
    • (1997) Mol. Biol. Cell , vol.8 , pp. 663-673
    • Murata, K.1    Hirano, K.2    Villa-Moruzzi, E.3    Hartshorne, D.J.4    Brautigan, D.L.5
  • 20
    • 0242456727 scopus 로고    scopus 로고
    • MAP kinase modules: Many roads home
    • Raman, M. and Cobb, M. H. (2003) MAP kinase modules: many roads home. Curr. Biol. 13, R886-R888
    • (2003) Curr. Biol , vol.13
    • Raman, M.1    Cobb, M.H.2
  • 21
    • 33747792064 scopus 로고    scopus 로고
    • MAPK signaling: ERK5 versus ERK1/2
    • Nishimoto, S. and Nishida, E. (2003) MAPK signaling: ERK5 versus ERK1/2. EMBO Rep. 7, 782-786
    • (2003) EMBO Rep , vol.7 , pp. 782-786
    • Nishimoto, S.1    Nishida, E.2
  • 22
    • 32144436881 scopus 로고    scopus 로고
    • Regulation of cellular functions by the ERK5 signalling pathway
    • Wang, X. and Tournier, C. (2006) Regulation of cellular functions by the ERK5 signalling pathway. Cell. Signalling 18, 753-760
    • (2006) Cell. Signalling , vol.18 , pp. 753-760
    • Wang, X.1    Tournier, C.2
  • 23
    • 25444485680 scopus 로고    scopus 로고
    • Transcriptional regulation of tissue-specific genes by the ERK5 mitogen-activated protein kinase
    • Sohn, S. J., Li, D., Lee, L. K. and Winoto, A. (2005) Transcriptional regulation of tissue-specific genes by the ERK5 mitogen-activated protein kinase. Mol Cell. Biol. 25, 8553-8566
    • (2005) Mol Cell. Biol , vol.25 , pp. 8553-8566
    • Sohn, S.J.1    Li, D.2    Lee, L.K.3    Winoto, A.4
  • 24
    • 0036133133 scopus 로고    scopus 로고
    • Erk5 participates in neuregulin signal transduction and is constitutively active in breast cancer cells overexpressing ErbB2
    • Esparis-Ogando, A., Diaz-Rodriguez, E., Montera, J. C., Yuste, L., Crespo, P. and Pandiella, A. (2002) Erk5 participates in neuregulin signal transduction and is constitutively active in breast cancer cells overexpressing ErbB2. Mol. Cell. Biol. 22, 270-285
    • (2002) Mol. Cell. Biol , vol.22 , pp. 270-285
    • Esparis-Ogando, A.1    Diaz-Rodriguez, E.2    Montera, J.C.3    Yuste, L.4    Crespo, P.5    Pandiella, A.6
  • 25
    • 18844438135 scopus 로고    scopus 로고
    • Activation of either ERK1/2 or ERK5 MAP kinase pathways can lead to disruption of the actin cytoskeleton
    • Barros, J. C. and Marshall, C. J. (2005) Activation of either ERK1/2 or ERK5 MAP kinase pathways can lead to disruption of the actin cytoskeleton. J. Cell Sci. 118, 1663-1671
    • (2005) J. Cell Sci , vol.118 , pp. 1663-1671
    • Barros, J.C.1    Marshall, C.J.2
  • 26
    • 0021104279 scopus 로고
    • Characterization of a reconstituted Mg-ATP-dependent protein phosphatase
    • Resink, T. J., Hemmings, B. A., Tung, H. Y. L. and Cohen, P. (1983) Characterization of a reconstituted Mg-ATP-dependent protein phosphatase. Eur. J. Biochem. 133, 455-461
    • (1983) Eur. J. Biochem , vol.133 , pp. 455-461
    • Resink, T.J.1    Hemmings, B.A.2    Tung, H.Y.L.3    Cohen, P.4
  • 27
    • 0025948991 scopus 로고
    • Determination of phosphoamino acid composition by acid hydrolysis of protein blotted to Immobilon
    • Kamps, P. M. (1991) Determination of phosphoamino acid composition by acid hydrolysis of protein blotted to Immobilon. Methods Enzymol. 201, 21-27
    • (1991) Methods Enzymol , vol.201 , pp. 21-27
    • Kamps, P.M.1
  • 28
    • 0031608439 scopus 로고    scopus 로고
    • Analyzing gene expression with the use of serine/threonine phosphatase inhibitors
    • Schoenthal, A. H. (1998) Analyzing gene expression with the use of serine/threonine phosphatase inhibitors. Methods Mol. Biol. 93, 35-40
    • (1998) Methods Mol. Biol , vol.93 , pp. 35-40
    • Schoenthal, A.H.1
  • 29
    • 16644396499 scopus 로고    scopus 로고
    • Analysis of isoform specific function of PP1 catalytic subunit in mammalian cells using siRNA
    • Okada, T., Fujii, T., Tanuma, N., Mitsuhashi, S., Urano, T., Araki, Y., Shima, H. and Kikuchi, K. (2004) Analysis of isoform specific function of PP1 catalytic subunit in mammalian cells using siRNA. Int. J. Oncol. 25, 1383-1388
    • (2004) Int. J. Oncol , vol.25 , pp. 1383-1388
    • Okada, T.1    Fujii, T.2    Tanuma, N.3    Mitsuhashi, S.4    Urano, T.5    Araki, Y.6    Shima, H.7    Kikuchi, K.8
  • 30
    • 1842831115 scopus 로고    scopus 로고
    • Use of inhibitors in the study of MAPK signaling
    • Schaul, Y. D. and Seger, R. (2004) Use of inhibitors in the study of MAPK signaling. Methods Mol. Biol. 250, 113-125
    • (2004) Methods Mol. Biol , vol.250 , pp. 113-125
    • Schaul, Y.D.1    Seger, R.2
  • 31
    • 0035958732 scopus 로고    scopus 로고
    • Effects of MAP kinase cascade inhibitors on the MKK5/ERK5 pathway
    • Mody, N., Leitch, J., Armstrong, C., Dixon, J. and Cohen, P. (2001) Effects of MAP kinase cascade inhibitors on the MKK5/ERK5 pathway. FEBS Lett. 502, 21-24
    • (2001) FEBS Lett , vol.502 , pp. 21-24
    • Mody, N.1    Leitch, J.2    Armstrong, C.3    Dixon, J.4    Cohen, P.5
  • 32
    • 0031901141 scopus 로고    scopus 로고
    • Protein kinase C and the cytoskeleton
    • Keenan, C. and Kelleher, D. (1998) Protein kinase C and the cytoskeleton. Cell. Signalling 10, 225-232
    • (1998) Cell. Signalling , vol.10 , pp. 225-232
    • Keenan, C.1    Kelleher, D.2
  • 33
    • 20944432633 scopus 로고    scopus 로고
    • Reciprocally interacting domains of protein phosphatase 1 and focal adhesion kinase
    • Bianchi, M., De Lucchini, S., Vietri, M. and Villa-Moruzzi, E. (2005) Reciprocally interacting domains of protein phosphatase 1 and focal adhesion kinase. Mol. Cell. Biochem. 272, 85-90
    • (2005) Mol. Cell. Biochem , vol.272 , pp. 85-90
    • Bianchi, M.1    De Lucchini, S.2    Vietri, M.3    Villa-Moruzzi, E.4
  • 34
    • 21244494930 scopus 로고    scopus 로고
    • G protein-coupled receptor activation rapidly stimulates focal adhesion kinase phosphorylation at Ser-843
    • Fan, R. S., Jacamo, R. O., Jang, S., Sinnett-Smith, J. and Rozengurt, E. (2005) G protein-coupled receptor activation rapidly stimulates focal adhesion kinase phosphorylation at Ser-843. J. Biol. Chem. 280, 24212-24220
    • (2005) J. Biol. Chem , vol.280 , pp. 24212-24220
    • Fan, R.S.1    Jacamo, R.O.2    Jang, S.3    Sinnett-Smith, J.4    Rozengurt, E.5
  • 35
    • 0037143091 scopus 로고    scopus 로고
    • Protein phosphatases regulates endothelial cell motility and both the phosphorylation and the stability of focal adhesion complexes
    • Young, M. R., Kolesiak, K. and Meisinger, J. (2002) Protein phosphatases regulates endothelial cell motility and both the phosphorylation and the stability of focal adhesion complexes. Int. J. Cancer 100, 276-282
    • (2002) Int. J. Cancer , vol.100 , pp. 276-282
    • Young, M.R.1    Kolesiak, K.2    Meisinger, J.3
  • 36
    • 0033853684 scopus 로고    scopus 로고
    • Time-dependent dephosphorylation through serine/threonine phosphatases is required for stable adhesion of highly and poorly metastatic HT-29 colon carcinoma cell lines to collagen
    • Haier, J. and Nicolson, G. L. (2000) Time-dependent dephosphorylation through serine/threonine phosphatases is required for stable adhesion of highly and poorly metastatic HT-29 colon carcinoma cell lines to collagen. Anticancer Res. 20, 2265-2271
    • (2000) Anticancer Res , vol.20 , pp. 2265-2271
    • Haier, J.1    Nicolson, G.L.2


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