메뉴 건너뛰기




Volumn 371, Issue 3, 2003, Pages 957-964

Protein-protein interactions involved in the recognition of p27 by E3 ubiquitin ligase

Author keywords

Cancer; Cks1; p27; Proteasome; Skp2; Ubiquitin

Indexed keywords

BIOASSAY; CELLS; DISSOCIATION; ENZYME INHIBITION; FLUORESCENCE; TUMORS;

EID: 0038583881     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021722     Document Type: Article
Times cited : (27)

References (29)
  • 1
    • 0028931265 scopus 로고
    • Principles of CDK regulation
    • Morgan, D. O. (1995) Principles of CDK regulation. Nature (London) 374, 131-134
    • (1995) Nature (London) , vol.374 , pp. 131-134
    • Morgan, D.O.1
  • 3
    • 0033564697 scopus 로고    scopus 로고
    • CDK inhibitors: Positive and negative regulators of G1-phase progression
    • Sherr, C. J. and Roberts, J. M. (1999) CDK inhibitors: positive and negative regulators of G1-phase progression. Genes Dev. 13, 1501-1512
    • (1999) Genes Dev. , vol.13 , pp. 1501-1512
    • Sherr, C.J.1    Roberts, J.M.2
  • 4
    • 0031048236 scopus 로고    scopus 로고
    • Increased proteasome-dependent degradation of the cyclin-dependent kinase inhibitor p27 in aggressive colorectal carcinomas
    • Loda, M., Cukor, B., Tam, S. W., Lavin, P., Fiorentino, M., Draetta, G. F., Jessup, J. M. and Pagano, M. (1997) Increased proteasome-dependent degradation of the cyclin-dependent kinase inhibitor p27 in aggressive colorectal carcinomas. Nat. Med. (N.Y.) 3, 152-154
    • (1997) Nat. Med. (N.Y.) , vol.3 , pp. 152-154
    • Loda, M.1    Cukor, B.2    Tam, S.W.3    Lavin, P.4    Fiorentino, M.5    Draetta, G.F.6    Jessup, J.M.7    Pagano, M.8
  • 6
    • 0034092911 scopus 로고    scopus 로고
    • Regulation of the cdk inhibitor p27 and its deregulation in cancer
    • Slingerland, J. and Pagano, M. (2000) Regulation of the cdk inhibitor p27 and its deregulation in cancer. J. Cell. Physiol. 183, 10-17
    • (2000) J. Cell. Physiol. , vol.183 , pp. 10-17
    • Slingerland, J.1    Pagano, M.2
  • 7
    • 0033135878 scopus 로고    scopus 로고
    • Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation
    • Montagnoli, A., Fiore, F., Eytan, E., Carrano, A. C., Draetta, G. F., Hershko, A. and Pagano, M. (1999) Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation. Genes Dev. 13, 1181-1189
    • (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
  • 8
    • 0032905150 scopus 로고    scopus 로고
    • kip1, a G1 cyclin-dependent kinase inhibitor, is dependent on CDK2 activity and the proteasome
    • kip1, a G1 cyclin-dependent kinase inhibitor, is dependent on CDK2 activity and the proteasome. Mol. Cell. Biol. 19, 1190-1201
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1190-1201
    • Nguyen, H.1    Gitig, D.M.2    Koff, A.3
  • 9
    • 0030847760 scopus 로고    scopus 로고
    • Phosphorylation-dependent degradation of the cyclin-dependent kinase inhibitor p27
    • Vlach, J., Hennecke, S. and Amati, B. (1997) Phosphorylation-dependent degradation of the cyclin-dependent kinase inhibitor p27. EMBO J. 16, 5334-5344
    • (1997) EMBO J. , vol.16 , pp. 5334-5344
    • Vlach, J.1    Hennecke, S.2    Amati, B.3
  • 11
    • 0033176887 scopus 로고    scopus 로고
    • SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
    • Carrano, A. C., Eytan, E., Hershko, A. and Pagano, M. (1999) SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27. Nat. Cell Biol. 1, 193-199
    • (1999) Nat. Cell Biol. , vol.1 , pp. 193-199
    • Carrano, A.C.1    Eytan, E.2    Hershko, A.3    Pagano, M.4
  • 14
    • 0030662523 scopus 로고    scopus 로고
    • F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex
    • Skowyra, D., Craig, K. L., Tyers, M., Elledge, S. J. and Harper, J. W. (1997) F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex. Cell 91, 209-219
    • (1997) Cell , vol.91 , pp. 209-219
    • Skowyra, D.1    Craig, K.L.2    Tyers, M.3    Elledge, S.J.4    Harper, J.W.5
  • 19
    • 0022573987 scopus 로고
    • The fission yeast cell cycle control gene cdc2: Isolation of a sequence suc1 that suppresses cdc2 mutant function
    • Hayles, J., Beach, D., Durkacz, B. and Nurse, P. (1986) The fission yeast cell cycle control gene cdc2: isolation of a sequence suc1 that suppresses cdc2 mutant function. Mol. Gen. Genet. 202, 291-293
    • (1986) Mol. Gen. Genet. , vol.202 , pp. 291-293
    • Hayles, J.1    Beach, D.2    Durkacz, B.3    Nurse, P.4
  • 20
    • 0024553955 scopus 로고
    • The Saccharomyces cerevisiae CKS1 gene, a homolog of the Schizosaccharomyces pombe suc1+ gene, encodes a subunit of the Cdc28 protein kinase complex
    • Hadwiger, J. A., Wittenberg, C., Mendenhall, M. D. and Reed, S. I. (1989) The Saccharomyces cerevisiae CKS1 gene, a homolog of the Schizosaccharomyces pombe suc1+ gene, encodes a subunit of the Cdc28 protein kinase complex. Mol. Cell. Biol. 9, 2034-2041
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2034-2041
    • Hadwiger, J.A.1    Wittenberg, C.2    Mendenhall, M.D.3    Reed, S.I.4
  • 21
    • 0030292994 scopus 로고    scopus 로고
    • Cell cycle: Reaching for a role for the Cks proteins
    • Pines, J. (1996) Cell cycle: reaching for a role for the Cks proteins. Curr. Biol. 6, 1399-1402
    • (1996) Curr. Biol. , vol.6 , pp. 1399-1402
    • Pines, J.1
  • 22
    • 0029918062 scopus 로고    scopus 로고
    • Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1
    • Bourne, Y., Watson, M. H., Hickey, M. J., Holmes, W., Rocque, W., Reed, S. I. and Tainer, J. A. (1996) Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1. Cell 84, 863-874
    • (1996) Cell , vol.84 , pp. 863-874
    • Bourne, Y.1    Watson, M.H.2    Hickey, M.J.3    Holmes, W.4    Rocque, W.5    Reed, S.I.6    Tainer, J.A.7
  • 23
    • 0028819212 scopus 로고
    • Crystallization and preliminary crystallographic study of human CksHs1: A cell cycle regulatory protein
    • Arvai, A. S., Bourne,Y., Williams, D., Reed, S. I. and Tainer, J. A. (1995) Crystallization and preliminary crystallographic study of human CksHs1: a cell cycle regulatory protein. Proteins 21, 70-73
    • (1995) Proteins , vol.21 , pp. 70-73
    • Arvai, A.S.1    Bourne, Y.2    Williams, D.3    Reed, S.I.4    Tainer, J.A.5
  • 25
    • 0034802615 scopus 로고    scopus 로고
    • Use of homogeneous time-resolved fluorescence energy transfer in the measurement of nuclear receptor activation
    • Zhou, G., Cummings, R., Hermes, J. and Moller, D. E. (2001) Use of homogeneous time-resolved fluorescence energy transfer in the measurement of nuclear receptor activation. Methods 25, 54-61
    • (2001) Methods , vol.25 , pp. 54-61
    • Zhou, G.1    Cummings, R.2    Hermes, J.3    Moller, D.E.4
  • 26
    • 0035810976 scopus 로고    scopus 로고
    • Protein destruction: Adapting roles for Cks proteins
    • Harper, J. W. (2001) Protein destruction: adapting roles for Cks proteins. Curr. Biol. 11, R431-R435
    • (2001) Curr. Biol. , vol.11
    • Harper, J.W.1
  • 27
    • 0038645438 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted
  • 29
    • 0032980308 scopus 로고    scopus 로고
    • The prognostic significance of altered cyclin-dependent kinase inhibitors in human cancer
    • Tsihlias, J., Kapusta, L. and Slingerland, J. (1999) The prognostic significance of altered cyclin-dependent kinase inhibitors in human cancer. Annu. Rev. Med. 50, 401-423
    • (1999) Annu. Rev. Med. , vol.50 , pp. 401-423
    • Tsihlias, J.1    Kapusta, L.2    Slingerland, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.