메뉴 건너뛰기




Volumn 281, Issue 2, 2002, Pages 190-196

TGF-β induced G1 cell cycle arrest requires the activity of the proteasome pathway

Author keywords

CDK; Cell cycle; Proteasomal inhibitors; TGF

Indexed keywords

CYCLIN D; DNA; GROWTH INHIBITOR; PROTEASOME; PROTEASOME INHIBITOR; PROTEIN; TRANSFORMING GROWTH FACTOR BETA;

EID: 0036999416     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.2002.5670     Document Type: Article
Times cited : (15)

References (36)
  • 1
    • 0025222517 scopus 로고
    • The transforming growth factor-β family
    • Massagué, J. (1990). The transforming growth factor-β family. Annu. Rev. Cell Biol. 6, 597-641.
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 597-641
    • Massagué, J.1
  • 2
    • 0025104027 scopus 로고
    • TGF-β stimulation and inhibition of cell proliferation: New mechanistic insights
    • Moses, H. L., Yang, E. Y., and Pietenpol, J. (1990). TGF-β stimulation and inhibition of cell proliferation: New mechanistic insights. Cell 63, 245-247.
    • (1990) Cell , vol.63 , pp. 245-247
    • Moses, H.L.1    Yang, E.Y.2    Pietenpol, J.3
  • 3
    • 0029868841 scopus 로고    scopus 로고
    • Negative regulation of cell growth by TGF-β
    • Polyak, K. (1996). Negative regulation of cell growth by TGF-β. Biochim. Biophys. Acta 1242, 185-199.
    • (1996) Biochim. Biophys. Acta , vol.1242 , pp. 185-199
    • Polyak, K.1
  • 4
    • 0028168242 scopus 로고
    • Ink4b is a potential effector of TGF-β-induced cell cycle arrest
    • Ink4b is a potential effector of TGF-β-induced cell cycle arrest. Nature 371, 257-261.
    • (1994) Nature , vol.371 , pp. 257-261
    • Hannon, G.J.1    Beach, D.2
  • 5
    • 0030614715 scopus 로고    scopus 로고
    • Kip1 coordinate their inhibitory interactions with cdk4 and ckd2
    • Kip1 coordinate their inhibitory interactions with cdk4 and ckd2. Genes Dev. 11, 492-503.
    • (1997) Genes Dev. , vol.11 , pp. 492-503
    • Reynisdóttir, I.1    Massagué, J.2
  • 6
    • 0025326725 scopus 로고
    • Growth inhibition by TGF-β linked to suppression of retinoblastoma protein phosphorylation
    • Laiho, M., DeCaprio, J. A., Ludlow, J. W., Livingston, D. M., and Massagué J. (1990). Growth inhibition by TGF-β linked to suppression of retinoblastoma protein phosphorylation. Cell 62, 175-185.
    • (1990) Cell , vol.62 , pp. 175-185
    • Laiho, M.1    DeCaprio, J.A.2    Ludlow, J.W.3    Livingston, D.M.4    Massagué, J.5
  • 9
    • 0027374766 scopus 로고
    • TGF-β inhibition of CDK4 synthesis is linked to cell cycle arrest
    • Ewen, M. E., Sluss, H. K., Whitehouse, L. L., and Livingston, D. M. (1993). TGF-β inhibition of CDK4 synthesis is linked to cell cycle arrest. Cell 74, 1009-1020.
    • (1993) Cell , vol.74 , pp. 1009-1020
    • Ewen, M.E.1    Sluss, H.K.2    Whitehouse, L.L.3    Livingston, D.M.4
  • 10
    • 0032938746 scopus 로고    scopus 로고
    • Hepatocyte growth factor releases mink epithelial cells from transforming growth factor β1-induced growth arrest by restoring Cdk6 expression and cyclin E-associated Cdk2 activity
    • Tsubari, M., Taipale, J., Tiihonen, E., Keski-Oja, J., and Laiho, M. (1999). Hepatocyte growth factor releases mink epithelial cells from transforming growth factor β1-induced growth arrest by restoring Cdk6 expression and cyclin E-associated Cdk2 activity. Mol. Cell. Biol. 19, 3654-3663.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3654-3663
    • Tsubari, M.1    Taipale, J.2    Tiihonen, E.3    Keski-Oja, J.4    Laiho, M.5
  • 11
    • 0035855661 scopus 로고    scopus 로고
    • Ectopic expression of Cdk6 circumvents transforming growth factor-β mediated growth inhibition
    • Zhang, F., Taipale, M., Heiskanen, A., and Laiho, M. (2001). Ectopic expression of Cdk6 circumvents transforming growth factor-β mediated growth inhibition. Oncogene 20, 5888-5896.
    • (2001) Oncogene , vol.20 , pp. 5888-5896
    • Zhang, F.1    Taipale, M.2    Heiskanen, A.3    Laiho, M.4
  • 12
    • 0030978315 scopus 로고    scopus 로고
    • Repression of the CDK activator Cdc25A and cell-cycle arrest by cytokine TGF-β in cells lacking the CDK inhibitor p15
    • Iavarone, A., and Massagué, J. (1997). Repression of the CDK activator Cdc25A and cell-cycle arrest by cytokine TGF-β in cells lacking the CDK inhibitor p15. Nature 387, 417-422.
    • (1997) Nature , vol.387 , pp. 417-422
    • Iavarone, A.1    Massagué, J.2
  • 13
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • Ciechanover, A. (1998). The ubiquitin-proteasome pathway: On protein death and cell life. EMBO J. 17, 7151-7160.
    • (1998) EMBO J. , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 14
    • 0033016291 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and pathogenesis of human diseases
    • Schwartz, A. L., and Ciechanover, A. (1999). The ubiquitin-proteasome pathway and pathogenesis of human diseases. Annu. Rev. Med. 50, 57-74.
    • (1999) Annu. Rev. Med. , vol.50 , pp. 57-74
    • Schwartz, A.L.1    Ciechanover, A.2
  • 15
    • 0033813625 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis and human disease
    • Vu, P. K., and Sakamoto, K. M. (2000). Ubiquitin-mediated proteolysis and human disease. Mol. Genet. Metab. 71, 261-266.
    • (2000) Mol. Genet. Metab. , vol.71 , pp. 261-266
    • Vu, P.K.1    Sakamoto, K.M.2
  • 16
    • 0033257273 scopus 로고    scopus 로고
    • SMAD destruction turns off signalling
    • Heldin, C. H., and ten Dijke, P. (1999). SMAD destruction turns off signalling. Nat. Cell Biol. 1, E195-197.
    • (1999) Nat. Cell Biol. , vol.1
    • Heldin, C.H.1    Ten Dijke, P.2
  • 17
    • 0034654497 scopus 로고    scopus 로고
    • Controlling TGF-β signaling
    • Massagué, J., and Chen, Y.-G. (2000). Controlling TGF-β signaling. Genes Dev. 14, 627-644.
    • (2000) Genes Dev. , vol.14 , pp. 627-644
    • Massagué, J.1    Chen, Y.-G.2
  • 18
    • 0034785348 scopus 로고    scopus 로고
    • TGF-β signaling in tumor suppression and cancer progression
    • Derynck, R., Akhurst, R. J., and Balmain, A. (2001). TGF-β signaling in tumor suppression and cancer progression. Nat. Genet. 29, 117-129.
    • (2001) Nat. Genet. , vol.29 , pp. 117-129
    • Derynck, R.1    Akhurst, R.J.2    Balmain, A.3
  • 19
    • 0037063367 scopus 로고    scopus 로고
    • Proteasomal activity modulates TGF-β signaling in a gene-specific manner
    • Zhang, F., Mönkkönen, M., Roth, S., and Laiho, M. (2002). Proteasomal activity modulates TGF-β signaling in a gene-specific manner. FEBS Lett. 527, 58-62.
    • (2002) FEBS Lett. , vol.527 , pp. 58-62
    • Zhang, F.1    Mönkkönen, M.2    Roth, S.3    Laiho, M.4
  • 21
    • 0034715946 scopus 로고    scopus 로고
    • Proteasome inhibitors alter the orderly progression of DNA synthesis during S-phase in HeLa cells and lead to rereplication of DNA
    • Yamaguchi, R., and Dutta, A. (2000). Proteasome inhibitors alter the orderly progression of DNA synthesis during S-phase in HeLa cells and lead to rereplication of DNA. Exp. Cell Res. 261, 271-283.
    • (2000) Exp. Cell Res. , vol.261 , pp. 271-283
    • Yamaguchi, R.1    Dutta, A.2
  • 22
    • 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
  • 24
    • 0035966104 scopus 로고    scopus 로고
    • Degradation of p27(Kip1) at the G(0)-G(1) transition mediated by a Skp2-independent ubiquitination pathway
    • Hara, T., Kamura, T., Nakayama, K., Oshikawa, K., Hatakeyama, S., and Nakayama, K. (2001). Degradation of p27(Kip1) at the G(0)-G(1) transition mediated by a Skp2-independent ubiquitination pathway. J. Biol. Chem. 276, 48937-48943.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48937-48943
    • Hara, T.1    Kamura, T.2    Nakayama, K.3    Oshikawa, K.4    Hatakeyama, S.5    Nakayama, K.6
  • 25
    • 1342272916 scopus 로고    scopus 로고
    • How the cyclins became a cyclin: Regulated proteolysis in the cell cycle
    • Koepp, D. M., Harper, J. W., and Elledge, S. T. (1999). How the cyclins became a cyclin: Regulated proteolysis in the cell cycle. Cell 97, 431-434.
    • (1999) Cell , vol.97 , pp. 431-434
    • Koepp, D.M.1    Harper, J.W.2    Elledge, S.T.3
  • 26
    • 0035123105 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis of vertebrate G1- and S-phase regulators
    • Yew, P. R. (2001). Ubiquitin-mediated proteolysis of vertebrate G1- and S-phase regulators. J. Cell Physiol. 187, 1-10.
    • (2001) J. Cell Physiol. , vol.187 , pp. 1-10
    • Yew, P.R.1
  • 27
    • 0030845187 scopus 로고    scopus 로고
    • Differential interaction of the cyclin-dependent kinase (Cdk) inhibitor p27Kip1 with cyclin A-Cdk2 and cyclin D2-Cdk4
    • Blain, S. W., Montalvo, E., and Massague, J. (1997). Differential interaction of the cyclin-dependent kinase (Cdk) inhibitor p27Kip1 with cyclin A-Cdk2 and cyclin D2-Cdk4. J. Biol. Chem. 272, 25863-25872.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25863-25872
    • Blain, S.W.1    Montalvo, E.2    Massague, J.3
  • 28
    • 0034976149 scopus 로고    scopus 로고
    • TGF-β induces assembly of a Smad2-Smurf2 ubiquitin ligase complex that targets SnoN for degradation
    • Bonni, S., Wang, H., Causing, C. G., Kavsak, P., Stroschein, S. L., Luo, K., and Wrana, J. L. (2001). TGF-β induces assembly of a Smad2-Smurf2 ubiquitin ligase complex that targets SnoN for degradation. Nat. Cell Biol. 3, 587-595.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 587-595
    • Bonni, S.1    Wang, H.2    Causing, C.G.3    Kavsak, P.4    Stroschein, S.L.5    Luo, K.6    Wrana, J.L.7
  • 29
    • 0035498980 scopus 로고    scopus 로고
    • Smad3 recruits the anaphase-promoting complex for ubiquitination and degradation of SnoN
    • Stroschein, S. L., Bonni, S., Wrana, J. L., and Luo, K. (2001). Smad3 recruits the anaphase-promoting complex for ubiquitination and degradation of SnoN. Genes Dev. 15, 2822-2836.
    • (2001) Genes Dev. , vol.15 , pp. 2822-2836
    • Stroschein, S.L.1    Bonni, S.2    Wrana, J.L.3    Luo, K.4
  • 30
    • 0035930333 scopus 로고    scopus 로고
    • The anaphase-promoting complex mediates TGF-β signaling by targeting SnoN for destruction
    • Wan, Y., Liu, X., and Kirschner, M. W. (2001). The anaphase-promoting complex mediates TGF-β signaling by targeting SnoN for destruction. Mol. Cell 8, 1027-1039.
    • (2001) Mol. Cell , vol.8 , pp. 1027-1039
    • Wan, Y.1    Liu, X.2    Kirschner, M.W.3
  • 31
    • 0035754080 scopus 로고    scopus 로고
    • To cycle or not to cycle: A critical decision in cancer
    • Malumbres, M., and Barbacid, M. (2001). To cycle or not to cycle: A critical decision in cancer. Nat. Rev. Cancer 1, 222-231.
    • (2001) Nat. Rev. Cancer , vol.1 , pp. 222-231
    • Malumbres, M.1    Barbacid, M.2
  • 32
    • 0033786378 scopus 로고    scopus 로고
    • Rb function in cell-cycle regulation and apoptosis
    • Harbour, J. M., and Dean, D. C. (2000). Rb function in cell-cycle regulation and apoptosis. Nat. Cell Biol. 2, E65-67.
    • (2000) Nat. Cell Biol. , vol.2
    • Harbour, J.M.1    Dean, D.C.2
  • 33
    • 0030812809 scopus 로고    scopus 로고
    • Proteolysis and DNA replication: The CDC34 requirement in the Xenopus egg cell cycle
    • Yew, P. R., and Kirschner, M. (1997). Proteolysis and DNA replication: The CDC34 requirement in the Xenopus egg cell cycle. Science 277, 1672-1676.
    • (1997) Science , vol.277 , pp. 1672-1676
    • Yew, P.R.1    Kirschner, M.2
  • 35
    • 0036181371 scopus 로고    scopus 로고
    • Development of the proteasome inhibitor PS-341
    • Adams, J. (2002). Development of the proteasome inhibitor PS-341. Oncologist 7, 9-16.
    • (2002) Oncologist , vol.7 , pp. 9-16
    • Adams, J.1
  • 36
    • 0035180374 scopus 로고    scopus 로고
    • Ubiquitin proteasome pathway: Implications and advances in cancer therapy
    • Shah, S. A., Potter, M. W., and Callery, M. P. (2001). Ubiquitin proteasome pathway: Implications and advances in cancer therapy. Surg. Oncol. 10, 43-52.
    • (2001) Surg. Oncol. , vol.10 , pp. 43-52
    • Shah, S.A.1    Potter, M.W.2    Callery, M.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.