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Volumn 333, Issue 1, 2013, Pages 103-112

A novel CyclinE/CyclinA-CDK Inhibitor targets p27Kip1 degradation, cell cycle progression and cell survival: Implications in cancer therapy

Author keywords

Apoptosis; Cell cycle; CyclinE CyclinA CDK Inhibitor; Proliferation

Indexed keywords

CELL PENETRATING PEPTIDE; CYCLIN A; CYCLIN DEPENDENT KINASE 2; CYCLIN DEPENDENT KINASE INHIBITOR 1; CYCLIN DEPENDENT KINASE INHIBITOR 1A; CYCLIN E; RETINOBLASTOMA PROTEIN; THREONINE;

EID: 84876077100     PISSN: 03043835     EISSN: 18727980     Source Type: Journal    
DOI: 10.1016/j.canlet.2013.01.025     Document Type: Article
Times cited : (51)

References (34)
  • 1
    • 0029849620 scopus 로고    scopus 로고
    • Cancer cell cycles
    • Sherr C.J. Cancer cell cycles. Science 1996, 274:1672-1677.
    • (1996) Science , vol.274 , pp. 1672-1677
    • Sherr, C.J.1
  • 2
    • 0029119740 scopus 로고
    • Cell cycle control in mammalian cells: role of cyclins, cyclin dependent kinases (CDKs), growth suppressor genes and cyclin-dependent kinase inhibitors (CKIs)
    • Graña X., Reddy E.P. Cell cycle control in mammalian cells: role of cyclins, cyclin dependent kinases (CDKs), growth suppressor genes and cyclin-dependent kinase inhibitors (CKIs). Oncogene 1995, 11:211-219.
    • (1995) Oncogene , vol.11 , pp. 211-219
    • Graña, X.1    Reddy, E.P.2
  • 3
    • 0030933277 scopus 로고    scopus 로고
    • Oncoprotein networks
    • Hunter T. Oncoprotein networks. Cell 1997, 88:333-346.
    • (1997) Cell , vol.88 , pp. 333-346
    • Hunter, T.1
  • 4
    • 0035754080 scopus 로고    scopus 로고
    • To cycle or not to cycle: a critical decision in cancer
    • Malumbres M., Barbacid M. To cycle or not to cycle: a critical decision in cancer. Nat. Rev. Cancer 2001, 1:222-231.
    • (2001) Nat. Rev. Cancer , vol.1 , pp. 222-231
    • Malumbres, M.1    Barbacid, M.2
  • 5
    • 0029921317 scopus 로고    scopus 로고
    • Genetic alterations of cyclins, cyclin-dependent kinases, and Cdk inhibitors in human cancer
    • Hall M., Peters G. Genetic alterations of cyclins, cyclin-dependent kinases, and Cdk inhibitors in human cancer. Adv. Cancer Res. 1996, 68:67-108.
    • (1996) Adv. Cancer Res. , vol.68 , pp. 67-108
    • Hall, M.1    Peters, G.2
  • 8
    • 0028363519 scopus 로고
    • P27, A novel inhibitor of G1 cyclin-Cdk protein kinase activity, is related to p21
    • Toyoshima H., Hunter T. p27, A novel inhibitor of G1 cyclin-Cdk protein kinase activity, is related to p21. Cell 1994, 78:67-74.
    • (1994) Cell , vol.78 , pp. 67-74
    • Toyoshima, H.1    Hunter, T.2
  • 9
    • 19444386764 scopus 로고    scopus 로고
    • Molecular basis for the specificity of p27 toward cyclin-dependent kinases that regulate cell division
    • Lacy E.R., Wang Y., Post J., Nourse A., Webb W., Mapelli M., et al. Molecular basis for the specificity of p27 toward cyclin-dependent kinases that regulate cell division. J. Mol. Biol. 2005, 349:764-773.
    • (2005) J. Mol. Biol. , vol.349 , pp. 764-773
    • Lacy, E.R.1    Wang, Y.2    Post, J.3    Nourse, A.4    Webb, W.5    Mapelli, M.6
  • 10
    • 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., et al. Increased proteasome-dependent degradation of the cyclin-dependent kinase inhibitor p27 in aggressive colorectal carcinomas. Nat. Med. 1997, 3:231-234.
    • (1997) Nat. Med. , vol.3 , pp. 231-234
    • Loda, M.1    Cukor, B.2    Tam, S.W.3    Lavin, P.4    Fiorentino, M.5    Draetta, G.F.6
  • 11
    • 0029024015 scopus 로고
    • Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27
    • Pagano M., Tam S.W., Theodoras A.M., Beer-Romero P., Del Sal G., Chau V., et al. Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27. Science 1995, 269:682-685.
    • (1995) Science , vol.269 , pp. 682-685
    • Pagano, M.1    Tam, S.W.2    Theodoras, A.M.3    Beer-Romero, P.4    Del Sal, G.5    Chau, V.6
  • 12
    • 0033553390 scopus 로고    scopus 로고
    • Down-regulation of p27(Kip1) by two mechanisms, ubiquitin-mediated degradation and proteolytic processing
    • Shirane M., Harumiya Y., Ishida N., Hirai A., Miyamoto C., Hatakeyama S., et al. Down-regulation of p27(Kip1) by two mechanisms, ubiquitin-mediated degradation and proteolytic processing. J. Biol. Chem. 1999, 274:13886-13893.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13886-13893
    • Shirane, M.1    Harumiya, Y.2    Ishida, N.3    Hirai, A.4    Miyamoto, C.5    Hatakeyama, S.6
  • 13
    • 0034092911 scopus 로고    scopus 로고
    • Regulation of the cdk inhibitor p27 and its deregulation in cancer
    • Slingerland J., Pagano M. Regulation of the cdk inhibitor p27 and its deregulation in cancer. J. Cell Physiol. 2000, 183:10-17.
    • (2000) J. Cell Physiol. , vol.183 , pp. 10-17
    • Slingerland, J.1    Pagano, M.2
  • 14
    • 0033176887 scopus 로고    scopus 로고
    • SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
    • Carrano A.C., Eytan E., Hershko A., Pagano M. SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27. Nat. Cell Biol. 1999, 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
  • 15
    • 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., et al. Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation. Genes Dev. 1999, 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
  • 16
    • 0030847760 scopus 로고    scopus 로고
    • Phosphorylation-dependent degradation of the cyclin-dependent kinase inhibitor p27
    • Vlach J., Hennecke S., Amati B. Phosphorylation-dependent degradation of the cyclin-dependent kinase inhibitor p27. EMBO J. 1997, 16:5334-5344.
    • (1997) EMBO J. , vol.16 , pp. 5334-5344
    • Vlach, J.1    Hennecke, S.2    Amati, B.3
  • 17
    • 33846268807 scopus 로고    scopus 로고
    • P27 Phosphorylation by Src regulates inhibition of cyclin E-Cdk2
    • Chu I., Sun J., Arnaout A., Kahn H., Hanna W., Narod S., et al. p27 Phosphorylation by Src regulates inhibition of cyclin E-Cdk2. Cell 2007, 128:281-294.
    • (2007) Cell , vol.128 , pp. 281-294
    • Chu, I.1    Sun, J.2    Arnaout, A.3    Kahn, H.4    Hanna, W.5    Narod, S.6
  • 18
    • 0035092687 scopus 로고    scopus 로고
    • The cell-cycle regulatory protein Cks1 is required for SCF(Skp2)-mediated ubiquitinylation of p27
    • Ganoth D., Bornstein G., Ko T.K., Larsen B., Tyers M., Pagano M., et al. The cell-cycle regulatory protein Cks1 is required for SCF(Skp2)-mediated ubiquitinylation of p27. Nat. Cell Biol. 2001, 3:321-324.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 321-324
    • Ganoth, D.1    Bornstein, G.2    Ko, T.K.3    Larsen, B.4    Tyers, M.5    Pagano, M.6
  • 20
    • 0344809977 scopus 로고    scopus 로고
    • ATP-site directed inhibitors of cyclin-dependent kinases
    • Gray N., Détivaud L., Doerig C., Meijer L. ATP-site directed inhibitors of cyclin-dependent kinases. Curr. Med. Chem. 1999, 6:859-875.
    • (1999) Curr. Med. Chem. , vol.6 , pp. 859-875
    • Gray, N.1    Détivaud, L.2    Doerig, C.3    Meijer, L.4
  • 21
  • 22
    • 0033551218 scopus 로고    scopus 로고
    • Tossing monkey wrenches into the clock: new ways of treating cancer
    • Lees J.A., Weinberg R.A. Tossing monkey wrenches into the clock: new ways of treating cancer. Proc. Natl. Acad. Sci. USA 1999, 96:4221-4223.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4221-4223
    • Lees, J.A.1    Weinberg, R.A.2
  • 24
    • 0035413607 scopus 로고    scopus 로고
    • Structural basis for control by phosphorylation
    • Johnson L.N., Lewis R.J. Structural basis for control by phosphorylation. Chem. Rev. 2001, 101:2209-2242.
    • (2001) Chem. Rev. , vol.101 , pp. 2209-2242
    • Johnson, L.N.1    Lewis, R.J.2
  • 25
    • 0034800665 scopus 로고    scopus 로고
    • Cyclin-dependent kinase inhibitors for treating cancer
    • Toogood P.L. Cyclin-dependent kinase inhibitors for treating cancer. Med. Res. Rev. 2001, 21:487-498.
    • (2001) Med. Res. Rev. , vol.21 , pp. 487-498
    • Toogood, P.L.1
  • 26
    • 84860390569 scopus 로고    scopus 로고
    • Inhibition of PDGF, TGF-β, and Abl signaling and reduction of liver fibrosis by the small molecule Bcr-Abl tyrosine kinase antagonist Nilotinib
    • Liu Y., Wang Z., Kwong S.Q., Lui E.L., Friedman S.L., Li F.R., et al. Inhibition of PDGF, TGF-β, and Abl signaling and reduction of liver fibrosis by the small molecule Bcr-Abl tyrosine kinase antagonist Nilotinib. J. Hepatol. 2011, 55:612-625.
    • (2011) J. Hepatol. , vol.55 , pp. 612-625
    • Liu, Y.1    Wang, Z.2    Kwong, S.Q.3    Lui, E.L.4    Friedman, S.L.5    Li, F.R.6
  • 27
    • 1842473094 scopus 로고    scopus 로고
    • P27 Binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding
    • Lacy E.R., Filippov I., Lewis W.S., Otieno S., Xiao L., Weiss S., et al. p27 Binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding. Nat. Struct. Mol. Biol. 2004, 11:358-364.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 358-364
    • Lacy, E.R.1    Filippov, I.2    Lewis, W.S.3    Otieno, S.4    Xiao, L.5    Weiss, S.6
  • 30
    • 84876072554 scopus 로고    scopus 로고
    • Discovery Studio, version 2.0; Accelrys: San Diego, CA
    • Discovery Studio, version 2.0; Accelrys: San Diego, CA, 2007.
    • (2007)
  • 31
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris G.M., Goodsell D.S., Halliday R.S., Huey R., Hart W.E., Belew R.K., et al. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comput. Chem. 1998, 19:1639-1662.
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6
  • 32
    • 33947362252 scopus 로고    scopus 로고
    • Small-molecule mimics of an α-helix for efficient transport of proteins into cells
    • Okuyama M., Laman H., Kingsbury S.R., Visintin C., Leo E., Eward K.L., et al. Small-molecule mimics of an α-helix for efficient transport of proteins into cells. Nat. Methods 2007, 4:153-159.
    • (2007) Nat. Methods , vol.4 , pp. 153-159
    • Okuyama, M.1    Laman, H.2    Kingsbury, S.R.3    Visintin, C.4    Leo, E.5    Eward, K.L.6
  • 33
    • 0030010591 scopus 로고    scopus 로고
    • Mice lacking p27(Kip1) display increased body size, multiple organ hyperplasia, retinal dysplasia, and pituitary tumors
    • Nakayama K., Ishida N., Shirane M., Inomata A., Inoue T., Shishido N., et al. Mice lacking p27(Kip1) display increased body size, multiple organ hyperplasia, retinal dysplasia, and pituitary tumors. Cell 1996, 85:707-720.
    • (1996) Cell , vol.85 , pp. 707-720
    • Nakayama, K.1    Ishida, N.2    Shirane, M.3    Inomata, A.4    Inoue, T.5    Shishido, N.6


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