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Volumn 287, Issue 52, 2012, Pages 43620-43629

Rho-associated coiled-coil kinase (ROCK) protein controls microtubule dynamics in a novel signaling pathway that regulates cell migration

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN DYNAMICS; CELL CYCLE; CELL MIGRATION; CELL MOTILITY; COILED COIL; HISTONE DEACETYLASES; MICROTUBULE DYNAMICS; MICROTUBULES; PROMOTING PROTEIN; SIGNALING PATHWAYS; TUBULIN POLYMERIZATION;

EID: 84871572775     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.394965     Document Type: Article
Times cited : (67)

References (40)
  • 2
    • 0034602959 scopus 로고    scopus 로고
    • Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop
    • DOI 10.1074/jbc.275.5.3577
    • Ohashi, K., Nagata, K., Maekawa, M., Ishizaki, T., Narumiya, S., and Mizuno, K. (2000) Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop. J. Biol. Chem. 275, 3577-3582 (Pubitemid 30083067)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.5 , pp. 3577-3582
    • Ohashi, K.1    Nagata, K.2    Maekawa, M.3    Ishizaki, T.4    Narumiya, S.5    Mizuno, K.6
  • 4
    • 0034984503 scopus 로고    scopus 로고
    • Stress fiber organization regulated by MLCK and Rho-kinase in cultured human fibroblasts
    • Katoh, K., Kano, Y., Amano, M., Kaibuchi, K., and Fujiwara, K. (2001) Stress fiber organization regulated by MLCK and Rho-kinase in cultured human fibroblasts. Am. J. Physiol. Cell Physiol. 280, C1669-1679
    • (2001) Am. J. Physiol. Cell Physiol. , vol.280
    • Katoh, K.1    Kano, Y.2    Amano, M.3    Kaibuchi, K.4    Fujiwara, K.5
  • 5
    • 0035808419 scopus 로고    scopus 로고
    • Specific activation of LIM kinase 2 via phosphorylation of threonine 505, by ROCK, a Rho-dependent protein kinase
    • DOI 10.1074/jbc.M007074200
    • Sumi, T., Matsumoto, K., and Nakamura, T. (2001) Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase. J. Biol. Chem. 276, 670-676 (Pubitemid 32050364)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.1 , pp. 670-676
    • Sumi, T.1    Matsumoto, K.2    Nakamura, T.3
  • 7
    • 0007354630 scopus 로고    scopus 로고
    • Rho-associated kinase phosphorylates desmin, the myogenic intermediate filament protein, at unique amino-terminal sites
    • DOI 10.1006/bbrc.1998.9732
    • Inada, H., Goto, H., Tanabe, K., Nishi, Y., Kaibuchi, K., and Inagaki, M. (1998) Rho-associated kinase phosphorylates desmin, the myogenic intermediate filament protein, at unique amino-terminal sites. Biochem. Biophys. Res. Commun. 253, 21-25 (Pubitemid 29015593)
    • (1998) Biochemical and Biophysical Research Communications , vol.253 , Issue.1 , pp. 21-25
    • Inada, H.1    Goto, H.2    Tanabe, K.3    Nishi, Y.4    Kaibuchi, K.5    Inagaki, M.6
  • 9
    • 0022452231 scopus 로고
    • The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules
    • Maruta, H., Greer, K., and Rosenbaum, J. L. (1986) The acetylation of α-tubulin and its relationship to the assembly and disassembly of microtubules. J. Cell Biol. 103, 571-579 (Pubitemid 16055052)
    • (1986) Journal of Cell Biology , vol.103 , Issue.2 , pp. 571-579
    • Maruta, H.1    Greer, K.2    Rosenbaum, J.L.3
  • 10
    • 0023293040 scopus 로고
    • Microtubules containing acetylated α-tubulin in mammalian cells in culture
    • Piperno, G., LeDizet, M., and Chang, X. J. (1987) Microtubules containing acetylated α-tubulin in mammalian cells in culture. J. Cell Biol. 104, 289-302
    • (1987) J. Cell Biol. , vol.104 , pp. 289-302
    • Piperno, G.1    LeDizet, M.2    Chang, X.J.3
  • 11
    • 78650731392 scopus 로고    scopus 로고
    • The major α-tubulin K40 acetyltransferase αTAT1 promotes rapid ciliogenesis and efficient mechanosensation
    • Shida, T., Cueva, J. G., Xu, Z., Goodman, M. B., and Nachury, M. V. (2010) The major α-tubulin K40 acetyltransferase αTAT1 promotes rapid ciliogenesis and efficient mechanosensation. Proc. Natl. Acad. Sci. U.S.A. 107, 21517-21522
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 21517-21522
    • Shida, T.1    Cueva, J.G.2    Xu, Z.3    Goodman, M.B.4    Nachury, M.V.5
  • 15
    • 0037291214 scopus 로고    scopus 로고
    • +-dependent tubulin deacetylase
    • DOI 10.1016/S1097-2765(03)00038-8
    • North, B. J., Marshall, B. L., Borra, M. T., Denu, J. M., and Verdin, E. (2003) The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol. Cell 11, 437-444 (Pubitemid 36293837)
    • (2003) Molecular Cell , vol.11 , Issue.2 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 16
    • 33750618516 scopus 로고    scopus 로고
    • Microtubule Acetylation Promotes Kinesin-1 Binding and Transport
    • DOI 10.1016/j.cub.2006.09.014, PII S096098220602207X
    • Reed, N. A., Cai, D., Blasius, T. L., Jih, G. T., Meyhofer, E., Gaertig, J., and Verhey, K. J. (2006) Microtubule acetylation promotes kinesin-1 binding and transport. Curr. Biol. 16, 2166-2172 (Pubitemid 44692098)
    • (2006) Current Biology , vol.16 , Issue.21 , pp. 2166-2172
    • Reed, N.A.1    Cai, D.2    Blasius, T.L.3    Jih, G.T.4    Meyhofer, E.5    Gaertig, J.6    Verhey, K.J.7
  • 17
    • 23744515800 scopus 로고    scopus 로고
    • A novel Rho-mDia2-HDAC6 pathway controls podosome patterning through microtubule acetylation in osteoclasts
    • DOI 10.1242/jcs.02425
    • Destaing, O., Saltel, F., Gilquin, B., Chabadel, A., Khochbin, S., Ory, S., and Jurdic, P. (2005) A novel Rho-mDia2-HDAC6 pathway controls podosome patterning through microtubule acetylation in osteoclasts. J. Cell Sci. 118, 2901-2911 (Pubitemid 41136367)
    • (2005) Journal of Cell Science , vol.118 , Issue.13 , pp. 2901-2911
    • Destaing, O.1    Saltel, F.2    Gilquin, B.3    Chabadel, A.4    Khochbin, S.5    Ory, S.6    Jurdic, P.7
  • 18
    • 79961133708 scopus 로고    scopus 로고
    • Microtubule remodelling is required for the front-rear polarity switch during contact inhibition of locomotion
    • Kadir, S., Astin, J. W., Tahtamouni, L., Martin, P., and Nobes, C. D. (2011) Microtubule remodelling is required for the front-rear polarity switch during contact inhibition of locomotion. J. Cell Sci. 124, 2642-2653
    • (2011) J. Cell Sci. , vol.124 , pp. 2642-2653
    • Kadir, S.1    Astin, J.W.2    Tahtamouni, L.3    Martin, P.4    Nobes, C.D.5
  • 19
    • 77649292108 scopus 로고    scopus 로고
    • Microtubules regulate migratory polarity through Rho/ROCK signaling in T cells
    • Takesono, A., Heasman, S. J., Wojciak-Stothard, B., Garg, R., and Ridley, A. J. (2010) Microtubules regulate migratory polarity through Rho/ROCK signaling in T cells. PLoS ONE 5, e8774
    • (2010) PLoS ONE , vol.5
    • Takesono, A.1    Heasman, S.J.2    Wojciak-Stothard, B.3    Garg, R.4    Ridley, A.J.5
  • 26
    • 84861211043 scopus 로고    scopus 로고
    • TPPP acts downstream of RhoA-ROCK-LIMK2 to regulate astral microtubule organization and spindle orientation
    • Heng, Y. W., Lim, H. H., Mina, T., Utomo, P., Zhong, S., Lim, C. T., and Koh, C. G. (2012) TPPP acts downstream of RhoA-ROCK-LIMK2 to regulate astral microtubule organization and spindle orientation. J. Cell Sci. 125, 1579-1590
    • (2012) J. Cell Sci. , vol.125 , pp. 1579-1590
    • Heng, Y.W.1    Lim, H.H.2    Mina, T.3    Utomo, P.4    Zhong, S.5    Lim, C.T.6    Koh, C.G.7
  • 28
    • 0031769792 scopus 로고    scopus 로고
    • Rapid hybridoma screening method for the identification of monoclonal antibodies to low-abundance cytoplasmic proteins
    • O'Reilly, L. A., Cullen, L., Moriishi, K., O'Connor, L., Huang, D. C., and Strasser, A. (1998) Rapid hybridoma screening method for the identification of monoclonal antibodies to low-abundance cytoplasmic proteins. BioTechniques 25, 824-830 (Pubitemid 28516506)
    • (1998) BioTechniques , vol.25 , Issue.5 , pp. 824-830
    • O'Reilly, L.A.1    Cullen, L.2    Moriishi, K.3    O'Connor, L.4    Huang, D.C.S.5    Strasser, A.6
  • 29
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko, A., Tomas, H., Havlis, J., Olsen, J. V., and Mann, M. (2006) In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1, 2856-2860
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 33
    • 0037047003 scopus 로고    scopus 로고
    • Brain-specific p25 protein binds to tubulin and microtubules and induces aberrant microtubule assemblies at substoichiometric concentrations
    • DOI 10.1021/bi020140g
    • Hlavanda, E., Kovács, J., Oláh, J., Orosz, F., Medzihradszky, K. F., and Ovádi, J. (2002) Brain-specific p25 protein binds to tubulin and microtubules and induces aberrant microtubule assemblies at substoichiometric concentrations. Biochemistry 41, 8657-8664 (Pubitemid 34743305)
    • (2002) Biochemistry , vol.41 , Issue.27 , pp. 8657-8664
    • Hlavanda, E.1    Kovacs, J.2    Olah, J.3    Orosz, F.4    Medzihradszky, K.F.5    Ovadi, J.6
  • 34
    • 29344451629 scopus 로고    scopus 로고
    • Chondroitinase ABC combined with neural stem/progenitor cell transplantation enhances graft cell migration and outgrowth of growth-associated protein-43-positive fibers after rat spinal cord injury
    • DOI 10.1111/j.1460-9568.2005.04492.x
    • Ikegami, T., Nakamura, M., Yamane, J., Katoh, H., Okada, S., Iwanami, A., Watanabe, K., Ishii, K., Kato, F., Fujita, H., Takahashi, T., Okano, H. J., Toyama, Y., and Okano, H. (2005) Chondroitinase ABC combined with neural stem/progenitor cell transplantation enhances graft cell migration and outgrowth of growth-associated protein-43-positive fibers after rat spinal cord injury. Eur. J. Neurosci. 22, 3036-3046 (Pubitemid 43001987)
    • (2005) European Journal of Neuroscience , vol.22 , Issue.12 , pp. 3036-3046
    • Ikegami, T.1    Nakamura, M.2    Yamane, J.3    Katoh, H.4    Okada, S.5    Iwanami, A.6    Watanabe, K.7    Ishii, K.8    Kato, F.9    Fujita, H.10    Takahashi, T.11    Okano, H.J.12    Toyama, Y.13    Okano, H.14
  • 35
    • 35748961107 scopus 로고    scopus 로고
    • Phosphorylation blocks the activity of tubulin polymerization-promoting protein (TPPP): Identification of sites targeted by different kinases
    • DOI 10.1074/jbc.M703466200
    • Hlavanda, E., Klement, E., Kókai, E., Kovács, J., Vincze, O., Tökési, N., Orosz, F., Medzihradszky, K. F., Dombrádi, V., and Ovádi, J. (2007) Phosphorylation blocks the activity of tubulin polymerization-promoting protein (TPPP). Identification of sites targeted by different kinases. J. Biol. Chem. 282, 29531-29539 (Pubitemid 350043337)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.40 , pp. 29531-29539
    • Hlavanda, E.1    Klement, E.2    Kokai, E.3    Kovacs, J.4    Vincze, O.5    Tokesi, N.6    Orosz, F.7    Medzihradszky, K.F.8    Dombradi, V.9    Ovadi, J.10
  • 36
  • 37
    • 84857036295 scopus 로고    scopus 로고
    • A novel GRK2/HDAC6 interaction modulates cell spreading and motility
    • Lafarga, V., Aymerich, I., Tapia, O., Mayor, F., Jr., and Penela, P. (2012) A novel GRK2/HDAC6 interaction modulates cell spreading and motility. EMBO J. 31, 856-869
    • (2012) EMBO J. , vol.31 , pp. 856-869
    • Lafarga, V.1    Aymerich, I.2    Tapia, O.3    Mayor Jr., F.4    Penela, P.5
  • 38
    • 22744446856 scopus 로고    scopus 로고
    • Significance of HDAC6 regulation via estrogen signaling for cell motility and prognosis in estrogen receptor-positive breast cancer
    • DOI 10.1038/sj.onc.1208646
    • Saji, S., Kawakami, M., Hayashi, S., Yoshida, N., Hirose, M., Horiguchi, S., Itoh, A., Funata, N., Schreiber, S. L., Yoshida, M., and Toi, M. (2005) Significance of HDAC6 regulation via estrogen signaling for cell motility and prognosis in estrogen receptor-positive breast cancer. Oncogene 24, 4531-4539 (Pubitemid 41032616)
    • (2005) Oncogene , vol.24 , Issue.28 , pp. 4531-4539
    • Saji, S.1    Kawakami, M.2    Hayashi, S.-I.3    Yoshida, N.4    Hirose, M.5    Horiguchi, S.-I.6    Itoh, A.7    Funata, N.8    Schreiber, S.L.9    Yoshida, M.10    Toi, M.11
  • 39
    • 61449123217 scopus 로고    scopus 로고
    • Rho/ROCK and MAPK signaling pathways are involved in glioblastoma cell migration and proliferation
    • Zohrabian, V. M., Forzani, B., Chau, Z., Murali, R., and Jhanwar-Uniyal, M. (2009) Rho/ROCK and MAPK signaling pathways are involved in glioblastoma cell migration and proliferation. Anticancer Res. 29, 119-123
    • (2009) Anticancer Res. , vol.29 , pp. 119-123
    • Zohrabian, V.M.1    Forzani, B.2    Chau, Z.3    Murali, R.4    Jhanwar-Uniyal, M.5
  • 40
    • 0141542627 scopus 로고    scopus 로고
    • Distinct mechanisms mediate the initial and sustained phases of cell migration in epidermal growth factor receptor-overexpressing cells
    • Kruger, J. S., and Reddy, K. B. (2003) Distinct mechanisms mediate the initial and sustained phases of cell migration in epidermal growth factor receptor-overexpressing cells. Mol. Cancer Res. 1, 801-809 (Pubitemid 37174451)
    • (2003) Molecular Cancer Research , vol.1 , Issue.11 , pp. 801-809
    • Kruger, J.S.1    Reddy, K.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.