메뉴 건너뛰기




Volumn 21, Issue 22, 2002, Pages 6061-6071

Dissection of c-MOS degron

Author keywords

c MOS; N end rule; Phosphorylation; Proteolysis; Ubiquitin

Indexed keywords

GLYCINE; LIGASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE; PROLINE; PROTEIN C MOS; SERINE; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 0037112776     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdf626     Document Type: Article
Times cited : (39)

References (35)
  • 2
    • 0024562943 scopus 로고
    • The degradation signal in a short-lived protein
    • Bachmair, A. and Varshavsky, A. (1989) The degradation signal in a short-lived protein. Cell, 56, 1019-1032.
    • (1989) Cell , vol.56 , pp. 1019-1032
    • Bachmair, A.1    Varshavsky, A.2
  • 3
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair, A., Finley, D. and Varshavsky, A. (1986) In vivo half-life of a protein is a function of its amino-terminal residue. Science, 234, 179-186.
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 4
    • 0032127904 scopus 로고    scopus 로고
    • N-terminal processing: The methionine aminopeptidase and Na-acetyl transferase families
    • Bradshaw, R.A., Brickey, W.W. and Walker, K.W. (1998) N-terminal processing: The methionine aminopeptidase and Na-acetyl transferase families. Trends Biochem. Sci., 23, 263-267.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 263-267
    • Bradshaw, R.A.1    Brickey, W.W.2    Walker, K.W.3
  • 6
    • 0037013862 scopus 로고    scopus 로고
    • A novel regulatory element determines the timing of Mos mRNA translation during Xenopus oocyte maturation
    • Charlesworth, A., Ridge, J.A., King, L.A., MacNicol, M.C. and MacNicol, A.M. (2002) A novel regulatory element determines the timing of Mos mRNA translation during Xenopus oocyte maturation. EMBO J., 21, 2798-2806.
    • (2002) EMBO J. , vol.21 , pp. 2798-2806
    • Charlesworth, A.1    Ridge, J.A.2    King, L.A.3    MacNicol, M.C.4    MacNicol, A.M.5
  • 7
    • 0034725661 scopus 로고    scopus 로고
    • RGS4 is arginylated and degraded by the N-end rule pathway in vitro
    • Davydov, I.V. and Varshavsky, A. (2000) RGS4 is arginylated and degraded by the N-end rule pathway in vitro. J. Biol. Chem., 275, 22931-22941.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22931-22941
    • Davydov, I.V.1    Varshavsky, A.2
  • 9
    • 0037171729 scopus 로고    scopus 로고
    • An arresting activity
    • Duesbery, N.S. and Vande Woude, G.F. (2002) An arresting activity. Nature, 416, 804-805.
    • (2002) Nature , vol.416 , pp. 804-805
    • Duesbery, N.S.1    Vande Woude, G.F.2
  • 10
    • 0036683056 scopus 로고    scopus 로고
    • Mos is not required for the initiation of meiotic maturation in Xenopus oocytes
    • Dupré, A., Jessus, C., Ozon, R. and Haccard, O. (2002) Mos is not required for the initiation of meiotic maturation in Xenopus oocytes. EMBO J., 21, 4026-4036.
    • (2002) EMBO J. , vol.21 , pp. 4026-4036
    • Dupré, A.1    Jessus, C.2    Ozon, R.3    Haccard, O.4
  • 11
    • 0033214147 scopus 로고    scopus 로고
    • Xenopus oocyte maturation: New lessons from a good egg
    • Ferrell, J.E. (1999) Xenopus oocyte maturation: New lessons from a good egg. BioEssays, 21, 833-842.
    • (1999) BioEssays , vol.21 , pp. 833-842
    • Ferrell, J.E.1
  • 12
    • 0036532226 scopus 로고    scopus 로고
    • Self-perpetuating states in signal transduction: Positive feedback, double-negative feedback and bistability
    • Ferrell, J.E. (2002) Self-perpetuating states in signal transduction: Positive feedback, double-negative feedback and bistability. Curr. Opin. Chem. Biol., 6, 140-148.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 140-148
    • Ferrell, J.E.1
  • 13
    • 0026585561 scopus 로고
    • Phosphorylation of conserved serine residues does not regulate the ability of mos protein to induce oocyte maturation or function as cytostatic factor
    • Freeman, R.S., Meyer, A.N., Li, J. and Donoghue, D.J. (1992) Phosphorylation of conserved serine residues does not regulate the ability of mos protein to induce oocyte maturation or function as cytostatic factor. J. Cell Biol., 116, 725-735.
    • (1992) J. Cell Biol. , vol.116 , pp. 725-735
    • Freeman, R.S.1    Meyer, A.N.2    Li, J.3    Donoghue, D.J.4
  • 15
    • 0020645064 scopus 로고
    • The use of Xenopus oocytes for the expression of cloned genes
    • Gurdon, J.B. and Wickens, M.P. (1983) The use of Xenopus oocytes for the expression of cloned genes. Methods Enzymol., 101, 370-386.
    • (1983) Methods Enzymol. , vol.101 , pp. 370-386
    • Gurdon, J.B.1    Wickens, M.P.2
  • 17
    • 0035166684 scopus 로고    scopus 로고
    • Construction and analysis of mouse strains lacking the ubiquitin ligase UBR1 (E3a) of the N-end rule pathway
    • Kwon, Y.T., Xia, Z., Davydov, I.V., Lecker, S.H. and Varshavsky, A. (2001) Construction and analysis of mouse strains lacking the ubiquitin ligase UBR1 (E3a) of the N-end rule pathway. Mol. Cell. Biol., 21, 8007-8021.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8007-8021
    • Kwon, Y.T.1    Xia, Z.2    Davydov, I.V.3    Lecker, S.H.4    Varshavsky, A.5
  • 19
    • 0034673706 scopus 로고    scopus 로고
    • Prosphorylation of CPE binding factor by Eg2 regulates translation of c-mos mRNA
    • Mendez, R., Hake, L.E., Andresson, T., Littlepage, L.E., Ruderman, J.V. and Richter, J.D. (2000) Prosphorylation of CPE binding factor by Eg2 regulates translation of c-mos mRNA. Nature, 404, 302-307.
    • (2000) Nature , vol.404 , pp. 302-307
    • Mendez, R.1    Hake, L.E.2    Andresson, T.3    Littlepage, L.E.4    Ruderman, J.V.5    Richter, J.D.6
  • 20
    • 0026266161 scopus 로고
    • Cell cycle extracts
    • Murray, A.W. (1991) Cell cycle extracts. Methods Cell Biol., 36, 581-605.
    • (1991) Methods Cell Biol. , vol.36 , pp. 581-605
    • Murray, A.W.1
  • 21
    • 0033724683 scopus 로고    scopus 로고
    • Regulation of the meiotic cell cycle in oocytes
    • Nebreda, A.R. and Ferby, I. (2000) Regulation of the meiotic cell cycle in oocytes. Curr. Opin. Cell Biol., 12, 666-675.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 666-675
    • Nebreda, A.R.1    Ferby, I.2
  • 22
    • 0026751110 scopus 로고
    • The second-codon rule and autophosphorylation govern the stability and activity of Mos during the meiotic cell cycle in Xenopus oocytes
    • Nishizawa, M., Okazaki, K., Furuno, N., Watanabe, N. and Sagata, N. (1992) The second-codon rule and autophosphorylation govern the stability and activity of Mos during the meiotic cell cycle in Xenopus oocytes. EMBO J., 11, 2433-2446.
    • (1992) EMBO J. , vol.11 , pp. 2433-2446
    • Nishizawa, M.1    Okazaki, K.2    Furuno, N.3    Watanabe, N.4    Sagata, N.5
  • 23
    • 0027264692 scopus 로고
    • Degradation of Mos by the N-terminal proline (Pro-2)-dependent ubiquitin pathway on fertilization of Xenopus eggs: Possible significance of natural selection for Pro-2 in Mos
    • Nishizawa, M., Furuno, N., Okazaki, K., Tanaka, H., Ogawa, Y. and Sagata, N. (1993) Degradation of Mos by the N-terminal proline (Pro-2)-dependent ubiquitin pathway on fertilization of Xenopus eggs: Possible significance of natural selection for Pro-2 in Mos. EMBO J., 12, 4021-4027.
    • (1993) EMBO J. , vol.12 , pp. 4021-4027
    • Nishizawa, M.1    Furuno, N.2    Okazaki, K.3    Tanaka, H.4    Ogawa, Y.5    Sagata, N.6
  • 24
    • 0033614969 scopus 로고    scopus 로고
    • Evidence for an important role of serine 16 and its phosphorylation in the stabilization of c-Mos
    • Pham, C.D., Vuyyuru, V.B., Yang, Y., Bai, W. and Singh, B. (1999) Evidence for an important role of serine 16 and its phosphorylation in the stabilization of c-Mos. Oncogene, 18, 4287-4294.
    • (1999) Oncogene , vol.18 , pp. 4287-4294
    • Pham, C.D.1    Vuyyuru, V.B.2    Yang, Y.3    Bai, W.4    Singh, B.5
  • 25
    • 0015924926 scopus 로고
    • Establishment of a cell line XTC-2 from the South American clawed toad Xenopus laevis
    • Pudney, M., Varma, M.G.R. and Leake, C.J. (1973) Establishment of a cell line XTC-2 from the South American clawed toad Xenopus laevis. Experientia, 29, 466-467.
    • (1973) Experientia , vol.29 , pp. 466-467
    • Pudney, M.1    Varma, M.G.R.2    Leake, C.J.3
  • 26
    • 0035912183 scopus 로고    scopus 로고
    • Degradation of a cohesin subunit by the N-end rule pathway is essential for chromosome stability
    • Rao, H., Uhlmann, F., Nasmyth, K. and Varshavsky, A. (2001) Degradation of a cohesin subunit by the N-end rule pathway is essential for chromosome stability. Nature, 410, 955-960.
    • (2001) Nature , vol.410 , pp. 955-960
    • Rao, H.1    Uhlmann, F.2    Nasmyth, K.3    Varshavsky, A.4
  • 27
    • 0037171734 scopus 로고    scopus 로고
    • Emil is required for cytostatic factor arrest in vertebrate eggs
    • Reimann, J.D.R. and Jackson, P.K. (2002) Emil is required for cytostatic factor arrest in vertebrate eggs. Nature, 416, 850-854.
    • (2002) Nature , vol.416 , pp. 850-854
    • Reimann, J.D.R.1    Jackson, P.K.2
  • 28
    • 0031015299 scopus 로고    scopus 로고
    • What does Mos do in oocytes and somatic cells?
    • Sagata, N. (1997) What does Mos do in oocytes and somatic cells? BioEssays, 19, 13-21.
    • (1997) BioEssays , vol.19 , pp. 13-21
    • Sagata, N.1
  • 29
    • 0024280269 scopus 로고
    • Function of c-mos proto-oncogene product in meiotic maturation of Xenopus oocytes
    • Sagata, N., Oskarsson, M., Copeland, T., Brumbaugh, J. and Vande Woude, G.F. (1988) Function of c-mos proto-oncogene product in meiotic maturation of Xenopus oocytes. Nature, 335, 519-525.
    • (1988) Nature , vol.335 , pp. 519-525
    • Sagata, N.1    Oskarsson, M.2    Copeland, T.3    Brumbaugh, J.4    Vande Woude, G.F.5
  • 31
    • 0033231281 scopus 로고    scopus 로고
    • Degradation signals in the lysine-asparagine sequence space
    • Suzuki, T. and Varshavsky, A. (1999) Degradation signals in the lysine-asparagine sequence space. EMBO J., 18, 6017-6026.
    • (1999) EMBO J. , vol.18 , pp. 6017-6026
    • Suzuki, T.1    Varshavsky, A.2
  • 32
    • 0034703437 scopus 로고    scopus 로고
    • Detecting and measuring cotranslational protein degradation in vivo
    • Turner, G.C. and Varshavsky, A. (2000) Detecting and measuring cotranslational protein degradation in vivo. Science, 289, 2117-2120.
    • (2000) Science , vol.289 , pp. 2117-2120
    • Turner, G.C.1    Varshavsky, A.2
  • 33
    • 0034213352 scopus 로고    scopus 로고
    • Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway
    • Turner, G.C., Du, F. and Varshavsky, A. (2000) Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway. Nature, 405, 579-583.
    • (2000) Nature , vol.405 , pp. 579-583
    • Turner, G.C.1    Du, F.2    Varshavsky, A.3
  • 34
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • Varshavsky, A. (1996) The N-end rule: Functions, mysteries, uses. Proc. Natl Acad. Sci. USA, 93, 12142-12149.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 35
    • 0034581529 scopus 로고    scopus 로고
    • Ubiquitin fusion technique and its descendants
    • Varshavsky, A. (2000) Ubiquitin fusion technique and its descendants. Methods Enzymol., 327, 578-593.
    • (2000) Methods Enzymol. , vol.327 , pp. 578-593
    • Varshavsky, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.