메뉴 건너뛰기




Volumn 2, Issue , 2008, Pages 79-87

MEKK1: Dual Function as a Protein Kinase and a Ubiquitin Protein Ligase

Author keywords

MEKK1; Protein kinase; Ubiquitin protein ligase

Indexed keywords


EID: 84889333374     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527620210.ch4     Document Type: Chapter
Times cited : (1)

References (43)
  • 1
    • 0037972167 scopus 로고    scopus 로고
    • Scores of RINGS but no PHDs in ubiquitin signaling
    • Aravind, L., L. M. Iyer, and E. V. Koonin. 2003. Scores of RINGS but no PHDs in ubiquitin signaling. Cell Cycle 2:123-6.
    • (2003) Cell Cycle , vol.2 , pp. 123-126
    • Aravind, L.1    Iyer, L.M.2    Koonin, E.V.3
  • 2
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • Blume-Jensen, P., and T. Hunter. 2001. Oncogenic kinase signalling. Nature 411:355-65.
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 3
    • 0034748469 scopus 로고    scopus 로고
    • MHC class I ubiquitìnation by a viral PHD/LAP finger protein
    • Boname, J. M., and P. G. Stevenson. 2001. MHC class I ubiquitìnation by a viral PHD/LAP finger protein. Immunity 15:627-36.
    • (2001) Immunity , vol.15 , pp. 627-636
    • Boname, J.M.1    Stevenson, P.G.2
  • 4
    • 0034602928 scopus 로고    scopus 로고
    • RING domains: master builders of molecular scaffolds?
    • Borden, K. L. 2000. RING domains: master builders of molecular scaffolds? J Mol Biol 295:1103-12.
    • (2000) J Mol Biol , vol.295 , pp. 1103-1112
    • Borden, K.L.1
  • 5
    • 0029977716 scopus 로고    scopus 로고
    • The RING finger domain: a recent example of a sequence-structure family
    • Borden, K. L., and P. S. Freemont. 1996. The RING finger domain: a recent example of a sequence-structure family. Curr Opin Struct Biol 6:395-401.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 395-401
    • Borden, K.L.1    Freemont, P.S.2
  • 6
    • 0035863152 scopus 로고    scopus 로고
    • Solution structure of the PHD domain from the KAP-1 corepressor: structural determinants for PHD, RING and LIM zinc-binding domains
    • Capili, A. D., D. C. Schultz, I. F. Rauscher, and K. L. Borden. 2001. Solution structure of the PHD domain from the KAP-1 corepressor: structural determinants for PHD, RING and LIM zinc-binding domains. Embo J 20:165-77.
    • (2001) Embo J , vol.20 , pp. 165-177
    • Capili, A.D.1    Schultz, D.C.2    Rauscher, I.F.3    Borden, K.L.4
  • 7
    • 0035863152 scopus 로고    scopus 로고
    • Solution structure of the PHD domain from the KAP-1 corepressor: structural determinants for PHD, RING and LIM zinc-binding domains
    • Capili, A. D., D. C. Schultz, I. F. Rauscher, and K. L. Borden. 2001. Solution structure of the PHD domain from the KAP-1 corepressor: structural determinants for PHD, RING and LIM zinc-binding domains. Embo J 20:165-77.
    • (2001) Embo J , vol.20 , pp. 165-177
    • Capili, A.D.1    Schultz, D.C.2    Rauscher, I.F.3    Borden, K.L.4
  • 8
    • 0033176887 scopus 로고    scopus 로고
    • SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
    • Carrano, A. C., E. Eytan, A. Hershko, and M. Pagano. 1999. SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27. Nat Cell Biol 1:193-9.
    • (1999) Nat Cell Biol , vol.1 , pp. 193-199
    • Carrano, A.C.1    Eytan, E.2    Hershko, A.3    Pagano, M.4
  • 9
    • 0037213013 scopus 로고    scopus 로고
    • PHD domains and E3 ubiquitin ligases: viruses make the connection
    • Coscoy, L., and D. Ganem. 2003. PHD domains and E3 ubiquitin ligases: viruses make the connection. Trends Cell Biol 13:7-12.
    • (2003) Trends Cell Biol , vol.13 , pp. 7-12
    • Coscoy, L.1    Ganem, D.2
  • 10
    • 11144246474 scopus 로고    scopus 로고
    • Reply to Scheel and Hofmann: Progressing towards a better definition of PHD domains
    • Coscoy, L., and D. Ganem. 2003. Reply to Scheel and Hofmann: Progressing towards a better definition of PHD domains. Trends Cell Biol 13:287-8.
    • (2003) Trends Cell Biol , vol.13 , pp. 287-288
    • Coscoy, L.1    Ganem, D.2
  • 11
    • 0035945349 scopus 로고    scopus 로고
    • A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition
    • Coscoy, L., D. J. Sanchez, and D. Ganem. 2001. A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition. J Cell Biol 155:1265-73.
    • (2001) J Cell Biol , vol.155 , pp. 1265-1273
    • Coscoy, L.1    Sanchez, D.J.2    Ganem, D.3
  • 12
    • 0033279836 scopus 로고    scopus 로고
    • SCF and Cullin/Ring H2-based ubiquitin ligases
    • Deshaies, R. J. 1999. SCF and Cullin/Ring H2-based ubiquitin ligases. Annu Rev Cell Dev Biol 15:435-67.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 13
    • 0034923514 scopus 로고    scopus 로고
    • Regulation of G protein-initiated signal transduction in yeast: paradigms and principles
    • Dohlman, H. G., and J. W. Thorner. 2001. Regulation of G protein-initiated signal transduction in yeast: paradigms and principles. Annu Rev Biochem 70:703-54.
    • (2001) Annu Rev Biochem , vol.70 , pp. 703-754
    • Dohlman, H.G.1    Thorner, J.W.2
  • 14
    • 0037047096 scopus 로고    scopus 로고
    • Pheromone induction promotes Ste11 degradation through a MAPK feedback and ubiquitin-dependent mechanism
    • Esch, R. K., and B. Errede. 2002. Pheromone induction promotes Ste11 degradation through a MAPK feedback and ubiquitin-dependent mechanism. Proc Natl Acad Sci U S A 99:9160-5.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 9160-9165
    • Esch, R.K.1    Errede, B.2
  • 15
    • 0242344011 scopus 로고    scopus 로고
    • The role of ubiquitin-proteasome pathway in oncogenic signaling
    • Fuchs, S. Y. 2002. The role of ubiquitin-proteasome pathway in oncogenic signaling. Cancer Biol Ther 1:337-41.
    • (2002) Cancer Biol Ther , vol.1 , pp. 337-341
    • Fuchs, S.Y.1
  • 16
    • 0038352134 scopus 로고    scopus 로고
    • c-MIR, a human E3 ubiquitin ligase, is a functional homolog of herpesvirus proteins MIR1 and MIR2 and has similar activity
    • Goto, E., S. Ishido, Y. Sato, S. Ohgimoto, K. Ohgimoto, M. Nagano-Fujii, and H. Hotta. 2003. c-MIR, a human E3 ubiquitin ligase, is a functional homolog of herpesvirus proteins MIR1 and MIR2 and has similar activity. J Biol Chem 278:14657-68.
    • (2003) J Biol Chem , vol.278 , pp. 14657-14668
    • Goto, E.1    Ishido, S.2    Sato, Y.3    Ohgimoto, S.4    Ohgimoto, K.5    Nagano-Fujii, M.6    Hotta, H.7
  • 17
    • 0035212589 scopus 로고    scopus 로고
    • The ups and downs of MEK kinase interactions
    • Hagemann, C., and J. L. Blank. 2001. The ups and downs of MEK kinase interactions. Cell Signal 13:863-75.
    • (2001) Cell Signal , vol.13 , pp. 863-875
    • Hagemann, C.1    Blank, J.L.2
  • 18
    • 0034614490 scopus 로고    scopus 로고
    • Signaling-2000 and beyond
    • Hunter, T. 2000. Signaling-2000 and beyond. Cell 100:113-27.
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 20
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson, E. S., P. C. Ma, I. M. Ota, and A. Varshavsky. 1995. A proteolytic pathway that recognizes ubiquitin as a degradation signal. J Biol Chem 270:17442-56.
    • (1995) J Biol Chem , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 21
    • 0034704153 scopus 로고    scopus 로고
    • MEKK1 binds raf-1 and the ERK2 cascade components
    • Karandikar, M., S. Xu, and M. H. Cobb. 2000. MEKK1 binds raf-1 and the ERK2 cascade components. J Biol Chem 275:40120-7.
    • (2000) J Biol Chem , vol.275 , pp. 40120-40127
    • Karandikar, M.1    Xu, S.2    Cobb, M.H.3
  • 22
    • 0034704153 scopus 로고    scopus 로고
    • MEKK1 binds raf-1 and the ERK2 cascade components
    • Karandikar, M., S. Xu, and M. H. Cobb. 2000. MEKK1 binds raf-1 and the ERK2 cascade components. J Biol Chem 275:40120-7.
    • (2000) J Biol Chem , vol.275 , pp. 40120-40127
    • Karandikar, M.1    Xu, S.2    Cobb, M.H.3
  • 24
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multi-ubiquitin chain assembly
    • Koegl, M., T. Hoppe, S. Schlenker, H. D. Ulrich, T. U. Mayer, and S. Jentsch. 1999. A novel ubiquitination factor, E4, is involved in multi-ubiquitin chain assembly. Cell 96: 635-44.
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 25
    • 0027215820 scopus 로고
    • A divergence in the MAP kinase regulatory network defined by MEK kinase and Raf
    • Lange-Carter, C. A., C. M. Pleiman, A. M. Gardner, K. J. Blumer, and G. L. Johnson. 1993. A divergence in the MAP kinase regulatory network defined by MEK kinase and Raf. Science 260:315-9.
    • (1993) Science , vol.260 , pp. 315-319
    • Lange-Carter, C.A.1    Pleiman, C.M.2    Gardner, A.M.3    Blumer, K.J.4    Johnson, G.L.5
  • 26
    • 0036279167 scopus 로고    scopus 로고
    • The PHD domain of MEKK1 acts as an E3 ubiquitin ligase and mediates ubiquitination and degradation of ERK1/2
    • Lu, Z., S. Xu, C. Joazeiro, M. H. Cobb, and T. Hunter. 2002. The PHD domain of MEKK1 acts as an E3 ubiquitin ligase and mediates ubiquitination and degradation of ERK1/2. Mol Cell 9:945-56.
    • (2002) Mol Cell , vol.9 , pp. 945-956
    • Lu, Z.1    Xu, S.2    Joazeiro, C.3    Cobb, M.H.4    Hunter, T.5
  • 29
    • 0037228216 scopus 로고    scopus 로고
    • The PHD/LAP-domain protein M153R of myxomavirus is a ubiquitin ligase that induces the rapid internalization and lysosomal destruction of CD4
    • Mansouri, M., E. Bartee, K. Gouveia, B. T. Hovey Nerenberg, J. Barrett, L. Thomas, G. Thomas, G. McFadden, and K. Fruh. 2003. The PHD/LAP-domain protein M153R of myxomavirus is a ubiquitin ligase that induces the rapid internalization and lysosomal destruction of CD4. J Virol 77:1427-40.
    • (2003) J Virol , vol.77 , pp. 1427-1440
    • Mansouri, M.1    Bartee, E.2    Gouveia, K.3    Hovey Nerenberg, B.T.4    Barrett, J.5    Thomas, L.6    Thomas, G.7    McFadden, G.8    Fruh, K.9
  • 30
    • 0033135878 scopus 로고    scopus 로고
    • Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation
    • Montagnoli, A., F. Fiore, E. Eytan, A. C. Carrano, G. F. Draetta, A. Hershko, and M. Pagano. 1999. Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation. Genes Dev 13:1181-9.
    • (1999) Genes Dev , vol.13 , pp. 1181-1189
    • Montagnoli, A.1    Fiore, F.2    Eytan, E.3    Carrano, A.C.4    Draetta, G.F.5    Hershko, A.6    Pagano, M.7
  • 31
    • 0034671463 scopus 로고    scopus 로고
    • Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor
    • Pascual, J., M. Martinez-Yamout, H. J. Dyson, and P. E. Wright. 2000. Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor. J Mol Biol 304:723-9.
    • (2000) J Mol Biol , vol.304 , pp. 723-729
    • Pascual, J.1    Martinez-Yamout, M.2    Dyson, H.J.3    Wright, P.E.4
  • 32
    • 0034671463 scopus 로고    scopus 로고
    • Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor
    • Pascual, J., M. Martinez-Yamout, H. J. Dyson, and P. E. Wright. 2000. Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor. J Mol Biol 304:723-9.
    • (2000) J Mol Biol , vol.304 , pp. 723-729
    • Pascual, J.1    Martinez-Yamout, M.2    Dyson, H.J.3    Wright, P.E.4
  • 33
    • 0033895709 scopus 로고    scopus 로고
    • Wnt signaling and cancer
    • Polakis, P. 2000. Wnt signaling and cancer. Genes Dev 14:1837-51.
    • (2000) Genes Dev , vol.14 , pp. 1837-1851
    • Polakis, P.1
  • 34
    • 0037683361 scopus 로고    scopus 로고
    • No evidence for PHD fingers as ubiquitin ligases
    • author reply 287-8.
    • Scheel, H., and K. Hofmann. 2003. No evidence for PHD fingers as ubiquitin ligases. Trends Cell Biol 13:285-7; author reply 287-8.
    • (2003) Trends Cell Biol , vol.13 , pp. 285-287
    • Scheel, H.1    Hofmann, K.2
  • 36
    • 0033578073 scopus 로고    scopus 로고
    • p27(Kipl) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27
    • Tsvetkov, L. M., K. H. Yeh, S. J. Lee, H. Sun, and H. Zhang. 1999. p27(Kipl) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27. Curr Biol 9:661-4.
    • (1999) Curr Biol , vol.9 , pp. 661-664
    • Tsvetkov, L.M.1    Yeh, K.H.2    Lee, S.J.3    Sun, H.4    Zhang, H.5
  • 38
    • 0030847760 scopus 로고    scopus 로고
    • Phosphorylation-dependent degradation of the cyclin-dependent kinase inhibitor p27
    • Viach, J., S. Hennecke, and B. Amati. 1997. Phosphorylation-dependent degradation of the cyclin-dependent kinase inhibitor p27. Embo J 16:5334-44.
    • (1997) Embo J , vol.16 , pp. 5334-5344
    • Viach, J.1    Hennecke, S.2    Amati, B.3
  • 39
    • 0037591222 scopus 로고    scopus 로고
    • Regulation of Ste7 ubiquitination by Ste11 phosphorylation and the Skp1-Cullin-F-box complex
    • Wang, Y., Q. Ge, D. Houston, J. Thorner, B. Errede, and H. G. Dohlman. 2003. Regulation of Ste7 ubiquitination by Ste11 phosphorylation and the Skp1-Cullin-F-box complex. J Biol Chem 278:22284-9.
    • (2003) J Biol Chem , vol.278 , pp. 22284-22289
    • Wang, Y.1    Ge, Q.2    Houston, D.3    Thorner, J.4    Errede, B.5    Dohlman, H.G.6
  • 40
    • 0037449717 scopus 로고    scopus 로고
    • Ubiquitylation of MEKK1 inhibits its phosphorylation of MKK1 and MKK4 and activation of the ERK1/2 and JNK pathways
    • Witowsky, J. A., and G. L. Johnson. 2003. Ubiquitylation of MEKK1 inhibits its phosphorylation of MKK1 and MKK4 and activation of the ERK1/2 and JNK pathways. J Biol Chem 278:1403-6.
    • (2003) J Biol Chem , vol.278 , pp. 1403-1406
    • Witowsky, J.A.1    Johnson, G.L.2
  • 41
    • 0029081006 scopus 로고
    • MEKK1 phosphorylates MEK1 and MEK2 but does not cause activation of mitogen-activated protein kinase
    • Xu, S., D. Robbins, J. Frost, A. Dang, C. Lange-Carter, and M. H. Cobb. 1995. MEKK1 phosphorylates MEK1 and MEK2 but does not cause activation of mitogen-activated protein kinase. Proc Natl Acad Sci U S A 92:6808-12.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 6808-6812
    • Xu, S.1    Robbins, D.2    Frost, J.3    Dang, A.4    Lange-Carter, C.5    Cobb, M.H.6
  • 42
    • 0029942952 scopus 로고    scopus 로고
    • Cloning of rat MEK kinase 1 cDNA reveals an endogenous membrane-associated 195-kDa protein with a large regulatory domain
    • Xu, S., D. J. Robbins, L. B. Christerson, J. M. English, C. A. Vanderbilt, and M. H. Cobb. 1996. Cloning of rat MEK kinase 1 cDNA reveals an endogenous membrane-associated 195-kDa protein with a large regulatory domain. Proc Natl Acad Sci U S A 93:5291-5.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 5291-5295
    • Xu, S.1    Robbins, D.J.2    Christerson, L.B.3    English, J.M.4    Vanderbilt, C.A.5    Cobb, M.H.6
  • 43
    • 0032483967 scopus 로고    scopus 로고
    • Role of MEKK1 in cell survival and activation of JNK and ERK pathways defined by targeted gene disruption
    • Yujiri, T., S. Sather, G. R. Fanger, and G. L. Johnson. 1998. Role of MEKK1 in cell survival and activation of JNK and ERK pathways defined by targeted gene disruption. Science 282:1911-4.
    • (1998) Science , vol.282 , pp. 1911-1914
    • Yujiri, T.1    Sather, S.2    Fanger, G.R.3    Johnson, G.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.