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Volumn 37, Issue 12, 2005, Pages 2513-2520

Sequence- and position-dependent tagging protects extracellular-regulated kinase 3 protein from 26S proteasome-mediated degradation

Author keywords

c Myc; ERK3; Stabilization; Tag; Ubiquitination

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; PROTEASOME; PROTEIN; PROTEIN KINASE;

EID: 25844514173     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2005.06.007     Document Type: Article
Times cited : (15)

References (23)
  • 1
    • 0034604520 scopus 로고    scopus 로고
    • Degradation of the Epstein-Barr virus latent membrane protein 1 (LMP1) by the ubiquitin-proteasome pathway. Targeting via ubiquitination of the N-terminal residue
    • S. Aviel, G. Winberg, M. Massucci, and A. Ciechanover Degradation of the Epstein-Barr virus latent membrane protein 1 (LMP1) by the ubiquitin-proteasome pathway. Targeting via ubiquitination of the N-terminal residue Journal of Biological Chemistry 275 2000 23491 23499
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 23491-23499
    • Aviel, S.1    Winberg, G.2    Massucci, M.3    Ciechanover, A.4
  • 2
    • 0025823448 scopus 로고
    • ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF
    • T.G. Boulton, S.H. Nye, D.J. Robbins, N.Y. Ip, E. Radziejewska, and S.D. Morgenbesser ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF Cell 65 1991 663 675
    • (1991) Cell , vol.65 , pp. 663-675
    • Boulton, T.G.1    Nye, S.H.2    Robbins, D.J.3    Ip, N.Y.4    Radziejewska, E.5    Morgenbesser, S.D.6
  • 3
    • 0032531925 scopus 로고    scopus 로고
    • A novel site for ubiquitination: The N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein
    • K. Breitschopf, E. Bengal, T. Ziv, A. Admon, and A. Ciechanover A novel site for ubiquitination: The N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein EMBO Journal 17 1998 5964 5973
    • (1998) EMBO Journal , vol.17 , pp. 5964-5973
    • Breitschopf, K.1    Bengal, E.2    Ziv, T.3    Admon, A.4    Ciechanover, A.5
  • 4
    • 2642558103 scopus 로고    scopus 로고
    • Lipid phosphate phosphatases dimerise, but this interaction is not required for in vivo activity
    • C. Burnett, P. Makridou, L. Hewlett, and K. Howard Lipid phosphate phosphatases dimerise, but this interaction is not required for in vivo activity BMC Biochemistry 5 2004 2
    • (2004) BMC Biochemistry , vol.5 , pp. 2
    • Burnett, C.1    Makridou, P.2    Hewlett, L.3    Howard, K.4
  • 5
    • 17544363814 scopus 로고    scopus 로고
    • Characterization of a protein kinase that phosphorylates serine 189 of the mitogen-activated protein kinase homolog ERK3
    • M. Cheng, E. Zhen, M.J. Robinson, D. Ebert, E. Goldsmith, and M.H. Cobb Characterization of a protein kinase that phosphorylates serine 189 of the mitogen-activated protein kinase homolog ERK3 Journal of Biological Chemistry 271 1996 12057 12062
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 12057-12062
    • Cheng, M.1    Zhen, E.2    Robinson, M.J.3    Ebert, D.4    Goldsmith, E.5    Cobb, M.H.6
  • 6
    • 3042796205 scopus 로고    scopus 로고
    • N-terminal ubiquitination of extracellular signal-regulated kinase 3 and p21 directs their degradation by the proteasome
    • P. Coulombe, G. Rodier, E. Bonneil, P. Thibault, and S. Meloche N-terminal ubiquitination of extracellular signal-regulated kinase 3 and p21 directs their degradation by the proteasome Molecular and Cellular Biology 24 2004 6140 6150
    • (2004) Molecular and Cellular Biology , vol.24 , pp. 6140-6150
    • Coulombe, P.1    Rodier, G.2    Bonneil, E.3    Thibault, P.4    Meloche, S.5
  • 7
    • 0038721214 scopus 로고    scopus 로고
    • Rapid turnover of extracellular signal-regulated kinase 3 by the ubiquitin-proteasome pathway defines a novel paradigm of mitogen-activated protein kinase regulation during cellular differentiation
    • P. Coulombe, G. Rodier, S. Pelletier, J. Pellerin, and S. Meloche Rapid turnover of extracellular signal-regulated kinase 3 by the ubiquitin-proteasome pathway defines a novel paradigm of mitogen-activated protein kinase regulation during cellular differentiation Molecular and Cellular Biology 23 2003 4542 4558
    • (2003) Molecular and Cellular Biology , vol.23 , pp. 4542-4558
    • Coulombe, P.1    Rodier, G.2    Pelletier, S.3    Pellerin, J.4    Meloche, S.5
  • 10
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • M.H. Glickman, and A. Ciechanover The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction Physiological Reviews 82 2002 373 428
    • (2002) Physiological Reviews , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 11
    • 0033969432 scopus 로고    scopus 로고
    • Cdc20 protein contains a destruction-box but, unlike Clb2, its proteolysisis not acutely dependent on the activity of anaphase-promoting complex
    • P.Y. Goh, H.H. Lim, and U. Surana Cdc20 protein contains a destruction-box but, unlike Clb2, its proteolysisis not acutely dependent on the activity of anaphase-promoting complex European Journal of Biochemistry 267 2000 434 449
    • (2000) European Journal of Biochemistry , vol.267 , pp. 434-449
    • Goh, P.Y.1    Lim, H.H.2    Surana, U.3
  • 12
    • 0029905354 scopus 로고    scopus 로고
    • Differential regulation of the MAP, SAP and RK/p38 kinases by Pyst1, a novel cytosolic dual-specificity phosphatase
    • L.A. Groom, A.A. Sneddon, D.R. Alessi, S. Dowd, and S.M. Keyse Differential regulation of the MAP, SAP and RK/p38 kinases by Pyst1, a novel cytosolic dual-specificity phosphatase EMBO Journal 15 1996 3621 3632
    • (1996) EMBO Journal , vol.15 , pp. 3621-3632
    • Groom, L.A.1    Sneddon, A.A.2    Alessi, D.R.3    Dowd, S.4    Keyse, S.M.5
  • 13
    • 3142658067 scopus 로고    scopus 로고
    • Synergistic activation of CREB-mediated transcription by forskolin and phorbol ester requires PKC and depends on the glutamine-rich Q2 transactivation domain
    • M. Johannessen, M.P. Delghandi, O.M. Seternes, B. Johansen, and U. Moens Synergistic activation of CREB-mediated transcription by forskolin and phorbol ester requires PKC and depends on the glutamine-rich Q2 transactivation domain Cellular Signalling 16 2004 1187 1199
    • (2004) Cellular Signalling , vol.16 , pp. 1187-1199
    • Johannessen, M.1    Delghandi, M.P.2    Seternes, O.M.3    Johansen, B.4    Moens, U.5
  • 14
    • 0142242155 scopus 로고    scopus 로고
    • Nuclear export of ERK3 by a CRM1-dependent mechanism regulates its inhibitory action on cell cycle progression
    • C. Julien, P. Coulombe, and S. Meloche Nuclear export of ERK3 by a CRM1-dependent mechanism regulates its inhibitory action on cell cycle progression Journal of Biological Chemistry 278 2003 42615 42624
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 42615-42624
    • Julien, C.1    Coulombe, P.2    Meloche, S.3
  • 15
    • 0014322388 scopus 로고
    • Enhancement of the infectivity of simian virus 40 deoxyribonucleic acid with diethylaminoethyl-dextran
    • J.H. McCutchan, and J.S. Pagano Enhancement of the infectivity of simian virus 40 deoxyribonucleic acid with diethylaminoethyl-dextran Journal of the National Cancer Institute 4 1968 351 357
    • (1968) Journal of the National Cancer Institute , vol.4 , pp. 351-357
    • McCutchan, J.H.1    Pagano, J.S.2
  • 16
    • 0034751731 scopus 로고    scopus 로고
    • Simian virus 40 large T-antigen, but not small T-antigen, trans-activates the human cytomegalovirus major immediate early promoter
    • U. Moens, M. Van Ghelue, A.K. Kristoffersen, B. Johansen, O.P. Rekvig, and M. Degre Simian virus 40 large T-antigen, but not small T-antigen, trans-activates the human cytomegalovirus major immediate early promoter Virus Genes 23 2001 215 226
    • (2001) Virus Genes , vol.23 , pp. 215-226
    • Moens, U.1    Van Ghelue, M.2    Kristoffersen, A.K.3    Johansen, B.4    Rekvig, O.P.5    Degre, M.6
  • 17
    • 0034735901 scopus 로고    scopus 로고
    • Degradation of the E7 human papillomavirus oncoprotein by the ubiquitin-proteasome system: Targeting via ubiquitination of the N-terminal residue
    • E. Reinstein, M. Scheffner, M. Oren, A. Ciechanover, and A. Schwartz Degradation of the E7 human papillomavirus oncoprotein by the ubiquitin-proteasome system: Targeting via ubiquitination of the N-terminal residue Oncogene 19 2000 5944 5950
    • (2000) Oncogene , vol.19 , pp. 5944-5950
    • Reinstein, E.1    Scheffner, M.2    Oren, M.3    Ciechanover, A.4    Schwartz, A.5
  • 18
    • 2942530310 scopus 로고    scopus 로고
    • ERK and p38 MAPK-activated protein kinases: A family of protein kinases with diverse biological functions
    • P.P. Roux, and J. Blenis ERK and p38 MAPK-activated protein kinases: A family of protein kinases with diverse biological functions Microbiological and Molecular Biology Reviews 68 2004 320 344
    • (2004) Microbiological and Molecular Biology Reviews , vol.68 , pp. 320-344
    • Roux, P.P.1    Blenis, J.2
  • 20
    • 0033311495 scopus 로고    scopus 로고
    • A dominant role for the Raf-MEK pathway in forskolin, 12-O-tetradecanoyl-phorbol acetate, and platelet-derived growth factor-induced CREB (cAMP-responsive element-binding protein) activation, uncoupled from serine 133 phosphorylation in NIH 3T3 cells
    • O.M. Seternes, B. Johansen, and U. Moens A dominant role for the Raf-MEK pathway in forskolin, 12-O-tetradecanoyl-phorbol acetate, and platelet-derived growth factor-induced CREB (cAMP-responsive element-binding protein) activation, uncoupled from serine 133 phosphorylation in NIH 3T3 cells Molecular Endocrinology 13 1999 1071 1083
    • (1999) Molecular Endocrinology , vol.13 , pp. 1071-1083
    • Seternes, O.M.1    Johansen, B.2    Moens, U.3
  • 21
  • 22
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain
    • M. Treier, L.M. Staszewski, and D. Bohmann Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain Cell 78 1994 787 798
    • (1994) Cell , vol.78 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.