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Volumn 126, Issue 24, 2013, Pages 5670-5680

Phosphorylation of moesin by jun n-terminal kinase is important for podosome rosette formation in srctransformed fibroblasts

Author keywords

ERM; JNK; Moesin; Phosphorylation; Podosome rosettes

Indexed keywords

ANTHRA[1,9 CD]PYRAZOL 6(2H) ONE; MOESIN; SHORT HAIRPIN RNA; STRESS ACTIVATED PROTEIN KINASE; THREONINE;

EID: 84890498350     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.134361     Document Type: Article
Times cited : (12)

References (50)
  • 1
    • 79952324408 scopus 로고    scopus 로고
    • Emerging role for ERM proteins in cell adhesion and migration
    • Arpin, M., Chirivino, D., Naba, A. and Zwaenepoel, I. (2011). Emerging role for ERM proteins in cell adhesion and migration. Cell Adh. Migr. 5, 199-206.
    • (2011) Cell Adh. Migr. , vol.5 , pp. 199-206
    • Arpin, M.1    Chirivino, D.2    Naba, A.3    Zwaenepoel, I.4
  • 2
    • 0034659526 scopus 로고    scopus 로고
    • Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism
    • Arthur, W. T., Petch, L. A. and Burridge, K. (2000). Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism. Curr. Biol. 10, 719-722.
    • (2000) Curr. Biol. , vol.10 , pp. 719-722
    • Arthur, W.T.1    Petch, L.A.2    Burridge, K.3
  • 4
    • 63849151166 scopus 로고    scopus 로고
    • LOK is a major ERM kinase in resting lymphocytes and regulates cytoskeletal rearrangement through ERM phosphorylation
    • Belkina, N. V., Liu, Y., Hao, J. J., Karasuyama, H. and Shaw, S. (2009). LOK is a major ERM kinase in resting lymphocytes and regulates cytoskeletal rearrangement through ERM phosphorylation. Proc. Natl. Acad. Sci. USA 106, 4707-4712.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 4707-4712
    • Belkina, N.V.1    Liu, Y.2    Hao, J.J.3    Karasuyama, H.4    Shaw, S.5
  • 5
    • 21844475890 scopus 로고    scopus 로고
    • Constitutively active cytoplasmic c-Jun N-terminal kinase 1 is a dominant regulator of dendritic architecture: role of microtubule-associated protein 2 as an effector
    • Björkblom, B., Ostman, N., Hongisto, V., Komarovski, V., Filén, J. J., Nyman, T. A., Kallunki, T., Courtney, M. J. and Coffey, E. T. (2005). Constitutively active cytoplasmic c-Jun N-terminal kinase 1 is a dominant regulator of dendritic architecture: role of microtubule-associated protein 2 as an effector. J. Neurosci. 25, 6350-6361.
    • (2005) J. Neurosci. , vol.25 , pp. 6350-6361
    • Björkblom, B.1    Ostman, N.2    Hongisto, V.3    Komarovski, V.4    Filén, J.J.5    Nyman, T.A.6    Kallunki, T.7    Courtney, M.J.8    Coffey, E.T.9
  • 6
    • 33845653234 scopus 로고    scopus 로고
    • Uses for JNK: the many and varied substrates of the c-Jun N-terminal kinases
    • Bogoyevitch, M. A. and Kobe, B. (2006). Uses for JNK: the many and varied substrates of the c-Jun N-terminal kinases. Microbiol. Mol. Biol. Rev. 70, 1061-1095.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 1061-1095
    • Bogoyevitch, M.A.1    Kobe, B.2
  • 7
    • 0035831463 scopus 로고    scopus 로고
    • CD44 interaction with c-Src kinase promotes cortactin-mediated cytoskeleton function and hyaluronic aciddependent ovarian tumor cell migration
    • Bourguignon, L. Y., Zhu, H., Shao, L. and Chen, Y. W. (2001). CD44 interaction with c-Src kinase promotes cortactin-mediated cytoskeleton function and hyaluronic aciddependent ovarian tumor cell migration. J. Biol. Chem. 276, 7327-7336.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7327-7336
    • Bourguignon, L.Y.1    Zhu, H.2    Shao, L.3    Chen, Y.W.4
  • 10
    • 75449112263 scopus 로고    scopus 로고
    • Aiming for invadopodia: organizing polarized delivery at sites of invasion
    • Caldieri, G. and Buccione, R. (2010). Aiming for invadopodia: organizing polarized delivery at sites of invasion. Trends Cell Biol. 20, 64-70.
    • (2010) Trends Cell Biol , vol.20 , pp. 64-70
    • Caldieri, G.1    Buccione, R.2
  • 12
    • 0346037264 scopus 로고    scopus 로고
    • JNK1 is required for maintenance of neuronal microtubules and controls phosphorylation of microtubule-associated proteins
    • Chang, L., Jones, Y., Ellisman, M. H., Goldstein, L. S. and Karin, M. (2003). JNK1 is required for maintenance of neuronal microtubules and controls phosphorylation of microtubule-associated proteins. Dev. Cell 4, 521-533.
    • (2003) Dev. Cell , vol.4 , pp. 521-533
    • Chang, L.1    Jones, Y.2    Ellisman, M.H.3    Goldstein, L.S.4    Karin, M.5
  • 13
    • 33745468872 scopus 로고    scopus 로고
    • Direct interaction of focal adhesion kinase (FAK) with Met is required for FAK to promote hepatocyte growth factor-induced cell invasion
    • Chen, S. Y. and Chen, H. C. (2006). Direct interaction of focal adhesion kinase (FAK) with Met is required for FAK to promote hepatocyte growth factor-induced cell invasion. Mol. Cell. Biol. 26, 5155-5167.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5155-5167
    • Chen, S.Y.1    Chen, H.C.2
  • 14
    • 33845313655 scopus 로고    scopus 로고
    • Gonadotropin-releasing hormone promotes ovarian cancer cell invasiveness through c-Jun NH2-terminal kinase-mediated activation of matrix metalloproteinase (MMP)-2 and MMP-9
    • Cheung, L. W., Leung, P. C. and Wong, A. S. (2006). Gonadotropin-releasing hormone promotes ovarian cancer cell invasiveness through c-Jun NH2-terminal kinase-mediated activation of matrix metalloproteinase (MMP)-2 and MMP-9. Cancer Res. 66, 10902-10910.
    • (2006) Cancer Res , vol.66 , pp. 10902-10910
    • Cheung, L.W.1    Leung, P.C.2    Wong, A.S.3
  • 15
    • 0034644522 scopus 로고    scopus 로고
    • Signal transduction by the JNK group of MAP kinases
    • Davis, R. J. (2000). Signal transduction by the JNK group of MAP kinases. Cell 103, 239-252.
    • (2000) Cell , vol.103 , pp. 239-252
    • Davis, R.J.1
  • 16
    • 0034503095 scopus 로고    scopus 로고
    • Direct binding of the Na - H exchanger NHE1 to ERM proteins regulates the cortical cytoskeleton and cell shape independently of H(+) translocation
    • Denker, S. P., Huang, D. C., Orlowski, J., Furthmayr, H. and Barber, D. L. (2000). Direct binding of the Na - H exchanger NHE1 to ERM proteins regulates the cortical cytoskeleton and cell shape independently of H(+) translocation. Mol. Cell 6, 1425-1436.
    • (2000) Mol. Cell , vol.6 , pp. 1425-1436
    • Denker, S.P.1    Huang, D.C.2    Orlowski, J.3    Furthmayr, H.4    Barber, D.L.5
  • 17
    • 38749128376 scopus 로고    scopus 로고
    • The tyrosine kinase activity of c-Src regulates actin dynamics and organization of podosomes in osteoclasts
    • Destaing, O., Sanjay, A., Itzstein, C., Horne, W. C., Toomre, D., De Camilli, P. and Baron, R. (2008). The tyrosine kinase activity of c-Src regulates actin dynamics and organization of podosomes in osteoclasts. Mol. Biol. Cell 19, 394-404.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 394-404
    • Destaing, O.1    Sanjay, A.2    Itzstein, C.3    Horne, W.C.4    Toomre, D.5    De Camilli, P.6    Baron, R.7
  • 18
    • 0242691046 scopus 로고    scopus 로고
    • AP-1: a double-edged sword in tumorigenesis
    • Eferl, R. and Wagner, E. F. (2003). AP-1: a double-edged sword in tumorigenesis. Nat. Rev. Cancer 3, 859-868.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 859-868
    • Eferl, R.1    Wagner, E.F.2
  • 20
    • 0032555599 scopus 로고    scopus 로고
    • Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). Regulation by phosphatidylinositol 4,5-bisphosphate
    • Heiska, L., Alfthan, K., Grönholm, M., Vilja, P., Vaheri, A. and Carpén, O. (1998). Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). Regulation by phosphatidylinositol 4, 5-bisphosphate. J. Biol. Chem. 273, 21893-21900.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21893-21900
    • Heiska, L.1    Alfthan, K.2    Grönholm, M.3    Vilja, P.4    Vaheri, A.5    Carpén, O.6
  • 21
    • 0038495741 scopus 로고    scopus 로고
    • JNK phosphorylates paxillin and regulates cell migration
    • Huang, C., Rajfur, Z., Borchers, C., Schaller, M. D. and Jacobson, K. (2003). JNK phosphorylates paxillin and regulates cell migration. Nature 424, 219-223.
    • (2003) Nature , vol.424 , pp. 219-223
    • Huang, C.1    Rajfur, Z.2    Borchers, C.3    Schaller, M.D.4    Jacobson, K.5
  • 22
    • 58849085553 scopus 로고    scopus 로고
    • Ezrin interacts with cortactin to form podosomal rosettes in pancreatic cancer cells
    • Kocher, H. M., Sandle, J., Mirza, T. A., Li, N. F. and Hart, I. R. (2009). Ezrin interacts with cortactin to form podosomal rosettes in pancreatic cancer cells. Gut 58, 271-284.
    • (2009) Gut , vol.58 , pp. 271-284
    • Kocher, H.M.1    Sandle, J.2    Mirza, T.A.3    Li, N.F.4    Hart, I.R.5
  • 23
    • 77956915812 scopus 로고    scopus 로고
    • Src-dependent phosphorylation of ROCK participates in regulation of focal adhesion dynamics
    • Lee, H. H., Tien, S. C., Jou, T. S., Chang, Y. C., Jhong, J. G. and Chang, Z. F. (2010). Src-dependent phosphorylation of ROCK participates in regulation of focal adhesion dynamics. J. Cell Sci. 123, 3368-3377.
    • (2010) J. Cell Sci. , vol.123 , pp. 3368-3377
    • Lee, H.H.1    Tien, S.C.2    Jou, T.S.3    Chang, Y.C.4    Jhong, J.G.5    Chang, Z.F.6
  • 24
    • 0032482323 scopus 로고    scopus 로고
    • Identification and functional analysis of the ezrin-binding site in the hyaluronan receptor
    • Legg, J. W. and Isacke, C. M. (1998). Identification and functional analysis of the ezrin-binding site in the hyaluronan receptor, CD44. Curr. Biol. 8, 705-708.
    • (1998) CD44. Curr. Biol. , vol.8 , pp. 705-708
    • Legg, J.W.1    Isacke, C.M.2
  • 25
    • 80054031825 scopus 로고    scopus 로고
    • Degrading devices: invadosomes in proteolytic cell invasion
    • Linder, S., Wiesner, C. and Himmel, M. (2011). Degrading devices: invadosomes in proteolytic cell invasion. Annu. Rev. Cell Dev. Biol. 27, 185-211.
    • (2011) Annu. Rev. Cell Dev. Biol. , vol.27 , pp. 185-211
    • Linder, S.1    Wiesner, C.2    Himmel, M.3
  • 27
    • 0038004740 scopus 로고    scopus 로고
    • Targeting JNK for therapeutic benefit: from junk to gold?
    • Manning, A. M. and Davis, R. J. (2003). Targeting JNK for therapeutic benefit: from junk to gold? Nat. Rev. Drug Discov. 2, 554-565.
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 554-565
    • Manning, A.M.1    Davis, R.J.2
  • 28
    • 0032498528 scopus 로고    scopus 로고
    • Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association
    • Matsui, T., Maeda, M., Doi, Y., Yonemura, S., Amano, M., Kaibuchi, K., Tsukita, S. and Tsukita, S. (1998). Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association. J. Cell Biol. 140, 647-657.
    • (1998) J. Cell Biol. , vol.140 , pp. 647-657
    • Matsui, T.1    Maeda, M.2    Doi, Y.3    Yonemura, S.4    Amano, M.5    Kaibuchi, K.6    Tsukita, S.7    Tsukita, S.8
  • 29
    • 79959541003 scopus 로고    scopus 로고
    • The 'ins' and 'outs' of podosomes and invadopodia: characteristics, formation and function
    • Murphy, D. A. and Courtneidge, S. A. (2011). The 'ins' and 'outs' of podosomes and invadopodia: characteristics, formation and function. Nat. Rev. Mol. Cell Biol. 12, 413-426.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 413-426
    • Murphy, D.A.1    Courtneidge, S.A.2
  • 31
    • 0032567361 scopus 로고    scopus 로고
    • Phosphorylation of moesin by rhoassociated kinase (Rho-kinase) plays a crucial role in the formation of microvilli-like structures
    • Oshiro, N., Fukata, Y. and Kaibuchi, K. (1998). Phosphorylation of moesin by rhoassociated kinase (Rho-kinase) plays a crucial role in the formation of microvilli-like structures. J. Biol. Chem. 273, 34663-34666.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34663-34666
    • Oshiro, N.1    Fukata, Y.2    Kaibuchi, K.3
  • 32
    • 80053944532 scopus 로고    scopus 로고
    • FAK is required for the assembly of podosome rosettes
    • Pan, Y. R., Chen, C. L. and Chen, H. C. (2011). FAK is required for the assembly of podosome rosettes. J. Cell Biol. 195, 113-129.
    • (2011) J. Cell Biol. , vol.195 , pp. 113-129
    • Pan, Y.R.1    Chen, C.L.2    Chen, H.C.3
  • 33
    • 84876091547 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase SHP2 suppresses podosome rosette formation in Srctransformed fibroblasts
    • Pan, Y. R., Cho, K. H., Lee, H. H., Chang, Z. F. and Chen, H. C. (2013). Protein tyrosine phosphatase SHP2 suppresses podosome rosette formation in Srctransformed fibroblasts. J. Cell Sci. 126, 657-666.
    • (2013) J. Cell Sci. , vol.126 , pp. 657-666
    • Pan, Y.R.1    Cho, K.H.2    Lee, H.H.3    Chang, Z.F.4    Chen, H.C.5
  • 34
  • 35
    • 0034697252 scopus 로고    scopus 로고
    • Phosphorylation of the p190 RhoGAP N-terminal domain by c-Src results in a loss of GTP binding activity
    • Roof, R. W., Dukes, B. D., Chang, J. H. and Parsons, S. J. (2000). Phosphorylation of the p190 RhoGAP N-terminal domain by c-Src results in a loss of GTP binding activity. FEBS Lett. 472, 117-121.
    • (2000) FEBS Lett , vol.472 , pp. 117-121
    • Roof, R.W.1    Dukes, B.D.2    Chang, J.H.3    Parsons, S.J.4
  • 36
    • 0030847406 scopus 로고    scopus 로고
    • Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization
    • Serrador, J. M., Alonso-Lebrero, J. L., del Pozo, M. A., Furthmayr, H., Schwartz-Albiez, R., Calvo, J., Lozano, F. and Sánchez-Madrid, F. (1997). Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization. J. Cell Biol. 138, 1409-1423.
    • (1997) J. Cell Biol. , vol.138 , pp. 1409-1423
    • Serrador, J.M.1    Alonso-Lebrero, J.L.2    del Pozo, M.A.3    Furthmayr, H.4    Schwartz-Albiez, R.5    Calvo, J.6    Lozano, F.7    Sánchez-Madrid, F.8
  • 38
    • 0032583447 scopus 로고    scopus 로고
    • Cterminal threonine phosphorylation activates ERM proteins to link the cell's cortical lipid bilayer to the cytoskeleton
    • Simons, P. C., Pietromonaco, S. F., Reczek, D., Bretscher, A. and Elias, L. (1998). Cterminal threonine phosphorylation activates ERM proteins to link the cell's cortical lipid bilayer to the cytoskeleton. Biochem. Biophys. Res. Commun. 253, 561-565.
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 561-565
    • Simons, P.C.1    Pietromonaco, S.F.2    Reczek, D.3    Bretscher, A.4    Elias, L.5
  • 40
    • 33745626457 scopus 로고    scopus 로고
    • Cortactin has an essential and specific role in osteoclast actin assembly
    • Tehrani, S., Faccio, R., Chandrasekar, I., Ross, F. P. and Cooper, J. A. (2006). Cortactin has an essential and specific role in osteoclast actin assembly. Mol. Biol. Cell 17, 2882-2895.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2882-2895
    • Tehrani, S.1    Faccio, R.2    Chandrasekar, I.3    Ross, F.P.4    Cooper, J.A.5
  • 41
    • 0033521010 scopus 로고    scopus 로고
    • Cortical actin organization: lessons from ERM (ezrin/radixin/moesin) proteins
    • Tsukita, S. and Yonemura, S. (1999). Cortical actin organization: lessons from ERM (ezrin/radixin/moesin) proteins. J. Biol. Chem. 274, 34507-34510.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34507-34510
    • Tsukita, S.1    Yonemura, S.2
  • 42
    • 0028229539 scopus 로고
    • ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons
    • Tsukita, S., Oishi, K., Sato, N., Sagara, J., Kawai, A. and Tsukita, S. (1994). ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons. J. Cell Biol. 126, 391-401.
    • (1994) J. Cell Biol. , vol.126 , pp. 391-401
    • Tsukita, S.1    Oishi, K.2    Sato, N.3    Sagara, J.4    Kawai, A.5    Tsukita, S.6
  • 44
    • 0032508714 scopus 로고    scopus 로고
    • A mammalian scaffold complex that selectively mediates MAP kinase activation
    • Whitmarsh, A. J., Cavanagh, J., Tournier, C., Yasuda, J. and Davis, R. J. (1998). A mammalian scaffold complex that selectively mediates MAP kinase activation. Science 281, 1671-1674.
    • (1998) Science , vol.281 , pp. 1671-1674
    • Whitmarsh, A.J.1    Cavanagh, J.2    Tournier, C.3    Yasuda, J.4    Davis, R.J.5
  • 45
    • 71249161927 scopus 로고    scopus 로고
    • IL-1beta induces MMP-9 expression via a Ca2+-dependent CaMKII/JNK/c-JUN cascade in rat brain astrocytes
    • Wu, C. Y., Hsieh, H. L., Sun, C. C. and Yang, C. M. (2009). IL-1beta induces MMP-9 expression via a Ca2+-dependent CaMKII/JNK/c-JUN cascade in rat brain astrocytes. Glia 57, 1775-1789.
    • (2009) Glia , vol.57 , pp. 1775-1789
    • Wu, C.Y.1    Hsieh, H.L.2    Sun, C.C.3    Yang, C.M.4
  • 46
    • 34548808142 scopus 로고    scopus 로고
    • Nuclear factor of activated T3 is a negative regulator of Ras-JNK1/2-AP-1 induced cell transformation
    • Yao, K., Cho, Y. Y., Bergen, H. R., III, Madden, B. J., Choi, B. Y., Ma, W. Y., Bode, A. M. and Dong, Z. (2007). Nuclear factor of activated T3 is a negative regulator of Ras-JNK1/2-AP-1 induced cell transformation. Cancer Res. 67, 8725-8735.
    • (2007) Cancer Res , vol.67 , pp. 8725-8735
    • Yao, K.1    Cho, Y.Y.2    Bergen III, H.R.3    Madden, B.J.4    Choi, B.Y.5    Ma, W.Y.6    Bode, A.M.7    Dong, Z.8
  • 47
    • 0032559637 scopus 로고    scopus 로고
    • Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2
    • Yonemura, S., Hirao, M., Doi, Y., Takahashi, N., Kondo, T., Tsukita, S. and Tsukita, S. (1998). Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2. J. Cell Biol. 140, 885-895.
    • (1998) J. Cell Biol. , vol.140 , pp. 885-895
    • Yonemura, S.1    Hirao, M.2    Doi, Y.3    Takahashi, N.4    Kondo, T.5    Tsukita, S.6    Tsukita, S.7
  • 48
    • 0032926177 scopus 로고    scopus 로고
    • Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion
    • Yu, Q. and Stamenkovic, I. (1999). Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion. Genes Dev. 13, 35-48.
    • (1999) Genes Dev , vol.13 , pp. 35-48
    • Yu, Q.1    Stamenkovic, I.2
  • 49
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis
    • Yu, Q. and Stamenkovic, I. (2000). Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev. 14, 163-176.
    • (2000) Genes Dev , vol.14 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2
  • 50
    • 0036468005 scopus 로고    scopus 로고
    • CD44 anchors the assembly of matrilysin/MMP-7 with heparin-binding epidermal growth factor precursor and ErbB4 and regulates female reproductive organ remodeling
    • Yu, W.H., Woessner, J. F., Jr, McNeish, J. D. and Stamenkovic, I. (2002). CD44 anchors the assembly of matrilysin/MMP-7 with heparin-binding epidermal growth factor precursor and ErbB4 and regulates female reproductive organ remodeling. Genes Dev. 16, 307-323.
    • (2002) Genes Dev , vol.16 , pp. 307-323
    • Yu, W.H.1    Woessner Jr., J.F.2    McNeish, J.D.3    Stamenkovic, I.4


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