메뉴 건너뛰기




Volumn 24, Issue 4, 2004, Pages 1736-1746

Human CNK1 Acts as a Scaffold Protein, Linking Rho and Ras Signal Transduction Pathways

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; CNK PROTEIN; GENE PRODUCT; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; MUTANT PROTEIN; PROTEIN HCNK1; PROTEIN KSR; PROTEIN P21; PROTEIN RALGDS; PROTEIN SERINE THREONINE KINASE; RAS PROTEIN; REGULATOR PROTEIN; RHO FACTOR; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; RHOPHILIN; SERUM RESPONSE FACTOR; UNCLASSIFIED DRUG;

EID: 0842325725     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.24.4.1736-1746.2004     Document Type: Article
Times cited : (70)

References (44)
  • 1
    • 0037155242 scopus 로고    scopus 로고
    • Critical contribution of linker proteins to Raf kinase activation
    • Anselmo, A. N., R. Bumeister, J. M. Thomas, and M. A. White. 2002. Critical contribution of linker proteins to Raf kinase activation. J. Biol. Chem. 277:5940-5943.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5940-5943
    • Anselmo, A.N.1    Bumeister, R.2    Thomas, J.M.3    White, M.A.4
  • 2
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • Bishop, A. L., and A. Hall. 2000. Rho GTPases and their effector proteins. Biochem. J. 348(Part 2):241-255.
    • (2000) Biochem. J. , vol.348 , Issue.PART 2 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 3
    • 0028786020 scopus 로고
    • A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases
    • Burbelo, P. D., D. Drechsel, and A. Hall. 1995. A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases. J. Biol. Chem. 270:29071-29074.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29071-29074
    • Burbelo, P.D.1    Drechsel, D.2    Hall, A.3
  • 5
    • 0035171566 scopus 로고    scopus 로고
    • Regulation of the Forkhead transcription factor AFX by Ral-dependent phosphorylation of threonines 447 and 451
    • De Ruiter, N. D., B. M. Burgering, and J. L. Bos. 2001. Regulation of the Forkhead transcription factor AFX by Ral-dependent phosphorylation of threonines 447 and 451. Mol. Cell. Biol. 21:8225-8235.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8225-8235
    • De Ruiter, N.D.1    Burgering, B.M.2    Bos, J.L.3
  • 6
    • 0029121466 scopus 로고
    • In vitro binding assay for interactions of Rho and Rac with GTPase-activating proteins and effectors
    • Diekmann, D., and A. Hall. 1995. In vitro binding assay for interactions of Rho and Rac with GTPase-activating proteins and effectors. Methods Enzymol. 256:207-215.
    • (1995) Methods Enzymol. , vol.256 , pp. 207-215
    • Diekmann, D.1    Hall, A.2
  • 7
    • 0037182585 scopus 로고    scopus 로고
    • LIM kinase and Diaphanous cooperate to regulate serum response factor and actin dynamics
    • Geneste, O., J. W. Copeland, and R. Treisman. 2002. LIM kinase and Diaphanous cooperate to regulate serum response factor and actin dynamics. J. Cell Biol. 157:831-838.
    • (2002) J. Cell Biol. , vol.157 , pp. 831-838
    • Geneste, O.1    Copeland, J.W.2    Treisman, R.3
  • 8
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. 1998. Rho GTPases and the actin cytoskeleton. Science 279:509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 10
    • 0036191304 scopus 로고    scopus 로고
    • Rho GTPases in transformation and metastasis
    • Jaffe, A. B., and A. Hall. 2002. Rho GTPases in transformation and metastasis. Adv. Cancer Res. 84:57-80.
    • (2002) Adv. Cancer Res. , vol.84 , pp. 57-80
    • Jaffe, A.B.1    Hall, A.2
  • 11
    • 0036089476 scopus 로고    scopus 로고
    • HUGE: A database for human large proteins identified in the Kazusa cDNA sequencing project
    • Kikuno, R., T. Nagase, M. Waki, and O. Ohara. 2002. HUGE: a database for human large proteins identified in the Kazusa cDNA sequencing project. Nucleic Acids Res. 30:166-168.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 166-168
    • Kikuno, R.1    Nagase, T.2    Waki, M.3    Ohara, O.4
  • 12
    • 0037119386 scopus 로고    scopus 로고
    • Selective activation of small GTPase RhoA by tyrosine kinase Etk through its PH domain
    • Kim, O., J. Yang, and Y. Qiu. 2002. Selective activation of small GTPase RhoA by tyrosine kinase Etk through its PH domain. J. Biol. Chem. 277:30066-30071.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30066-30071
    • Kim, O.1    Yang, J.2    Qiu, Y.3
  • 14
    • 0035808389 scopus 로고    scopus 로고
    • Smooth muscle differentiation marker gene expression is regulated by RhoA-mediated actin polymerization
    • Mack, C. P., A. V. Somlyo, M. Hautmann, A. P. Somlyo, and G. K. Owens. 2001. Smooth muscle differentiation marker gene expression is regulated by RhoA-mediated actin polymerization. J. Biol. Chem. 276:341-347.
    • (2001) J. Biol. Chem. , vol.276 , pp. 341-347
    • Mack, C.P.1    Somlyo, A.V.2    Hautmann, M.3    Somlyo, A.P.4    Owens, G.K.5
  • 15
    • 0035281564 scopus 로고    scopus 로고
    • Regulation of gene expression by the small GTPase Rho through the ERK6 (p38 gamma) MAP kinase pathway
    • Marinissen, M. J., M. Chiariello, and J. S. Gutkind. 2001. Regulation of gene expression by the small GTPase Rho through the ERK6 (p38 gamma) MAP kinase pathway. Genes Dev. 15:535-553.
    • (2001) Genes Dev. , vol.15 , pp. 535-553
    • Marinissen, M.J.1    Chiariello, M.2    Gutkind, J.S.3
  • 16
    • 0028832520 scopus 로고
    • GTP hydrolysis by Ran occurs at the nuclear pore complex in an early step of protein import
    • Melchior, F., T. Guan, N. Yokoyama, T. Nishimoto, and L. Gerace. 1995. GTP hydrolysis by Ran occurs at the nuclear pore complex in an early step of protein import. J. Cell Biol. 131:571-581.
    • (1995) J. Cell Biol. , vol.131 , pp. 571-581
    • Melchior, F.1    Guan, T.2    Yokoyama, N.3    Nishimoto, T.4    Gerace, L.5
  • 17
    • 0038737042 scopus 로고    scopus 로고
    • Actin dynamics control SRF activity by regulation of its coactivator MAL
    • Miralles, F., G. Posern, A. I. Zaromytidou, and R. Treisman. 2003. Actin dynamics control SRF activity by regulation of its coactivator MAL. Cell 113:329-342.
    • (2003) Cell , vol.113 , pp. 329-342
    • Miralles, F.1    Posern, G.2    Zaromytidou, A.I.3    Treisman, R.4
  • 18
    • 0035018017 scopus 로고    scopus 로고
    • KSR: A MAPK scaffold of the Ras pathway?
    • Morrison, D. K. 2001. KSR: a MAPK scaffold of the Ras pathway? J. Cell Sci. 114:1609-1612.
    • (2001) J. Cell Sci. , vol.114 , pp. 1609-1612
    • Morrison, D.K.1
  • 20
    • 0027183541 scopus 로고
    • The PH domain: A common piece in the structural patchwork of signalling proteins
    • Musacchio, A., T. Gibson, P. Rice, J. Thompson, and M. Saraste. 1993. The PH domain: a common piece in the structural patchwork of signalling proteins. Trends Biochem. Sci. 18:343-348.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 343-348
    • Musacchio, A.1    Gibson, T.2    Rice, P.3    Thompson, J.4    Saraste, M.5
  • 21
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases control polarity, protrusion, and adhesion during cell movement
    • Nobes, C. D., and A. Hall. 1999. Rho GTPases control polarity, protrusion, and adhesion during cell movement. J. Cell Biol. 144:1235-1244.
    • (1999) J. Cell Biol. , vol.144 , pp. 1235-1244
    • Nobes, C.D.1    Hall, A.2
  • 22
    • 0037113916 scopus 로고    scopus 로고
    • The RhoA-binding protein, Rhophilin-2, regulates actin cytoskeleton organization
    • Peck, J. W., M. Oberst, K. B. Bouker, E. Bowden, and P. D. Burbelo. 2002. The RhoA-binding protein, Rhophilin-2, regulates actin cytoskeleton organization. J. Biol. Chem. 277:43924-43932.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43924-43932
    • Peck, J.W.1    Oberst, M.2    Bouker, K.B.3    Bowden, E.4    Burbelo, P.D.5
  • 23
    • 0029039613 scopus 로고
    • Pleckstrin homology domain-mediated membrane association and activation of the beta-adrenergic receptor kinase requires coordinate interaction with G beta gamma subunits and lipid
    • Pitcher, J. A., K. Touhara, E. S. Payne, and R. J. Lefkowitz. 1995. Pleckstrin homology domain-mediated membrane association and activation of the beta-adrenergic receptor kinase requires coordinate interaction with G beta gamma subunits and lipid. J. Biol. Chem. 270:11707-11710.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11707-11710
    • Pitcher, J.A.1    Touhara, K.2    Payne, E.S.3    Lefkowitz, R.J.4
  • 24
    • 0031171361 scopus 로고    scopus 로고
    • PDZ domains: Targeting signalling molecules to sub-membranous sites
    • Ponting, C. P., C. Phillips, K. E. Davies, and D. J. Blake. 1997. PDZ domains: targeting signalling molecules to sub-membranous sites. Bioessays 19:469-479.
    • (1997) Bioessays , vol.19 , pp. 469-479
    • Ponting, C.P.1    Phillips, C.2    Davies, K.E.3    Blake, D.J.4
  • 25
    • 0036715018 scopus 로고    scopus 로고
    • Interactions between Ras1, dMyc, and dPI3K signaling in the developing Drosophila wing
    • Prober, D. A., and B. A. Edgar. 2002. Interactions between Ras1, dMyc, and dPI3K signaling in the developing Drosophila wing. Genes Dev. 16:2286-2299.
    • (2002) Genes Dev. , vol.16 , pp. 2286-2299
    • Prober, D.A.1    Edgar, B.A.2
  • 26
    • 0032473351 scopus 로고    scopus 로고
    • RhoA effector mutants reveal distinct effector pathways for cytoskeletal reorganization, SRF activation and transformation
    • Sahai, E., A. S. Alberts, and R. Treisman. 1998. RhoA effector mutants reveal distinct effector pathways for cytoskeletal reorganization, SRF activation and transformation. EMBO J. 17:1350-1361.
    • (1998) EMBO J. , vol.17 , pp. 1350-1361
    • Sahai, E.1    Alberts, A.S.2    Treisman, R.3
  • 27
    • 0036644975 scopus 로고    scopus 로고
    • Guanine nucleotide exchange factors for Rho GTPases: Turning on the switch
    • Schmidt, A., and A. Hall. 2002. Guanine nucleotide exchange factors for Rho GTPases: turning on the switch. Genes Dev. 16:1587-1609.
    • (2002) Genes Dev. , vol.16 , pp. 1587-1609
    • Schmidt, A.1    Hall, A.2
  • 28
    • 0031022602 scopus 로고    scopus 로고
    • SAM as a protein interaction domain involved in developmental regulation
    • Schultz, J., C. P. Ponting, K. Hofmann, and P. Bork. 1997. SAM as a protein interaction domain involved in developmental regulation. Protein Sci. 6:249-253.
    • (1997) Protein Sci. , vol.6 , pp. 249-253
    • Schultz, J.1    Ponting, C.P.2    Hofmann, K.3    Bork, P.4
  • 29
    • 0033597825 scopus 로고    scopus 로고
    • Signal-regulated activation of serum response factor is mediated by changes in actin dynamics
    • Sotiropoulos, A., D. Gineitis, J. Copeland, and R. Treisman. 1999. Signal-regulated activation of serum response factor is mediated by changes in actin dynamics. Cell 98:159-169.
    • (1999) Cell , vol.98 , pp. 159-169
    • Sotiropoulos, A.1    Gineitis, D.2    Copeland, J.3    Treisman, R.4
  • 30
    • 0036141434 scopus 로고    scopus 로고
    • The exocyst complex binds the small GTPase RalA to mediate filopodia formation
    • Sugihara, K., S. Asano, K. Tanaka, A. Iwamatsu, K. Okawa, and Y. Ohta. 2002. The exocyst complex binds the small GTPase RalA to mediate filopodia formation. Nat. Cell Biol. 4:73-78.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 73-78
    • Sugihara, K.1    Asano, S.2    Tanaka, K.3    Iwamatsu, A.4    Okawa, K.5    Ohta, Y.6
  • 31
    • 0029559183 scopus 로고
    • The C. elegans ksr-1 gene encodes a novel Raf-related kinase involved in Ras-mediated signal transduction
    • Sundaram, M., and M. Han. 1995. The C. elegans ksr-1 gene encodes a novel Raf-related kinase involved in Ras-mediated signal transduction. Cell 83:889-901.
    • (1995) Cell , vol.83 , pp. 889-901
    • Sundaram, M.1    Han, M.2
  • 32
    • 0032473569 scopus 로고    scopus 로고
    • A new rac target POSH is an SH3-containing scaffold protein involved in the JNK and NF-kappaB signalling pathways
    • Tapon, N., K. Nagata, N. Lamarche, and A. Hall. 1998. A new rac target POSH is an SH3-containing scaffold protein involved in the JNK and NF-kappaB signalling pathways. EMBO J. 17:1395-1404.
    • (1998) EMBO J. , vol.17 , pp. 1395-1404
    • Tapon, N.1    Nagata, K.2    Lamarche, N.3    Hall, A.4
  • 35
    • 0032582663 scopus 로고    scopus 로고
    • CNK, a RAF-binding multidomain protein required for RAS signaling
    • Therrien, M., A. M. Wong, and G. M. Rubin. 1998. CNK, a RAF-binding multidomain protein required for RAS signaling. Cell 95:343-353.
    • (1998) Cell , vol.95 , pp. 343-353
    • Therrien, M.1    Wong, A.M.2    Rubin, G.M.3
  • 39
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst, L., and C. D'Souza-Schorey. 1997. Rho GTPases and signaling networks. Genes Dev. 11:2295-2322.
    • (1997) Genes Dev. , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 40
    • 0033522118 scopus 로고    scopus 로고
    • Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: Implications for nuclear transport
    • Vetter, I. R., C. Nowak, T. Nishimoto, J. Kuhlmann, and A. Wittinghofer. 1999. Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport. Nature 398:39-46.
    • (1999) Nature , vol.398 , pp. 39-46
    • Vetter, I.R.1    Nowak, C.2    Nishimoto, T.3    Kuhlmann, J.4    Wittinghofer, A.5
  • 41
    • 0033160196 scopus 로고    scopus 로고
    • Cooperation between mDial and ROCK in Rho-induced actin reorganization
    • Watanabe, N., T. Kato, A. Fujita, T. Ishizaki, and S. Narumiya. 1999. Cooperation between mDial and ROCK in Rho-induced actin reorganization. Nat. Cell Biol. 1:136-143.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 136-143
    • Watanabe, N.1    Kato, T.2    Fujita, A.3    Ishizaki, T.4    Narumiya, S.5
  • 44
    • 0032572698 scopus 로고    scopus 로고
    • Effector domain mutants of Rho dissociate cytoskeletal changes from nuclear signaling and cellular transformation
    • Zohar, M., H. Teramoto, B. Z. Katz, K. M. Yamada, and J. S. Gutkind. 1998. Effector domain mutants of Rho dissociate cytoskeletal changes from nuclear signaling and cellular transformation. Oncogene. 17:991-998.
    • (1998) Oncogene , vol.17 , pp. 991-998
    • Zohar, M.1    Teramoto, H.2    Katz, B.Z.3    Yamada, K.M.4    Gutkind, J.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.