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Volumn 20, Issue 8, 2006, Pages

HSP27 favors ubiquitination and proteasomal degradation of p27 Kip1 and helps S-phase re-entry in stressed cells

Author keywords

Cell death; Cell proliferation; Proteasome; Stress proteins; Ubiquitin

Indexed keywords

CYCLIN DEPENDENT KINASE INHIBITOR 1B; GLYCERYL TRINITRATE; HEAT SHOCK PROTEIN 27; NITRIC OXIDE; PROTEASOME; S PHASE KINASE ASSOCIATED PROTEIN 2; SERINE; THREONINE; HEAT SHOCK PROTEIN; HSPB1 PROTEIN, HUMAN; S PHASE KINASE ASSOCIATED PROTEIN; TUMOR PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE;

EID: 33845623275     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.05-4184fje     Document Type: Article
Times cited : (100)

References (56)
  • 1
    • 0029365005 scopus 로고
    • Modulation of actin dynamics during stress and physiological stimulation by a signaling pathway involving p38 MAP kinase and heat shock protein 27
    • Landry, J., and Huot, J. (1995) Modulation of actin dynamics during stress and physiological stimulation by a signaling pathway involving p38 MAP kinase and heat shock protein 27. Biochem. Cell Biol. 73, 703-707
    • (1995) Biochem. Cell Biol. , vol.73 , pp. 703-707
    • Landry, J.1    Huot, J.2
  • 3
    • 0034609765 scopus 로고    scopus 로고
    • Differential regulation of HSP27 oligomerization in tumor cells grown in vitro and in vivo
    • Bruey, J. M., Paul, C., Fromentin, A., Hilpert, S., Arrigo, A. P., Solary, E., and Garrido, C. (2000) Differential regulation of HSP27 oligomerization in tumor cells grown in vitro and in vivo. Oncogene 19, 4855-4863
    • (2000) Oncogene , vol.19 , pp. 4855-4863
    • Bruey, J.M.1    Paul, C.2    Fromentin, A.3    Hilpert, S.4    Arrigo, A.P.5    Solary, E.6    Garrido, C.7
  • 6
    • 0037239023 scopus 로고    scopus 로고
    • Small heat shock proteins participate in the regulation of cellular aggregates of misfolded protein
    • Ito, H., Inaguma, Y., and Kato, K. (2003) Small heat shock proteins participate in the regulation of cellular aggregates of misfolded protein. Nippon Yakurigaku Zasshi 121, 27-32
    • (2003) Nippon Yakurigaku Zasshi , vol.121 , pp. 27-32
    • Ito, H.1    Inaguma, Y.2    Kato, K.3
  • 8
    • 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
  • 10
    • 0033578073 scopus 로고    scopus 로고
    • p27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27
    • Tsvetkov, L. M., Yeh, K. H., Lee, S. J., Sun, H., and Zhang, H. (1999) p27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27. Curr. Biol. 9, 661-664
    • (1999) Curr. Biol. , vol.9 , pp. 661-664
    • Tsvetkov, L.M.1    Yeh, K.H.2    Lee, S.J.3    Sun, H.4    Zhang, H.5
  • 12
    • 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
  • 13
    • 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., and Hershko, A. (2001) The cell-cycle regulatory protein Cks1 is required for SCF(Skp2)-mediated ubiquitinylation of p27. Nat. Cell Biol. 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    Hershko, A.7
  • 14
    • 0035265829 scopus 로고    scopus 로고
    • A CDK-independent function of mammalian Cks1: Targeting of SCF(Skp2) to the CDK inhibitor p27Kip1
    • Spruck, C., Strohmaier, H., Watson, M., Smith, A. P., Ryan, A., Krek, T. W., and Reed, S. I. (2001) A CDK-independent function of mammalian Cks1: targeting of SCF(Skp2) to the CDK inhibitor p27Kip1. Mol. Cell 7, 639-650
    • (2001) Mol. Cell , vol.7 , pp. 639-650
    • Spruck, C.1    Strohmaier, H.2    Watson, M.3    Smith, A.P.4    Ryan, A.5    Krek, T.W.6    Reed, S.I.7
  • 17
    • 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., and Hatakeyama, S. (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
  • 18
    • 0035803593 scopus 로고    scopus 로고
    • p27 cytoplasmic localization is regulated by phosphorylation on Ser10 and is not a prerequisite for its proteolysis
    • Rodier, G., Montagnoli, A., Di Marcotullio, L., Coulombe, P., Draetta, G. F., Pagano, M., and Meloche, S. (2001) p27 cytoplasmic localization is regulated by phosphorylation on Ser10 and is not a prerequisite for its proteolysis. EMBO J. 20, 6672-6682
    • (2001) EMBO J. , vol.20 , pp. 6672-6682
    • Rodier, G.1    Montagnoli, A.2    Di Marcotullio, L.3    Coulombe, P.4    Draetta, G.F.5    Pagano, M.6    Meloche, S.7
  • 19
    • 0037177386 scopus 로고    scopus 로고
    • Phosphorylation of p27Kip1 on serine 10 is required for its binding to CRM1 and nuclear export
    • Ishida, N., Hara, T., Kamura, T., Yoshida, M., Nakayama, K., and Nakayama, K. I. (2002) Phosphorylation of p27Kip1 on serine 10 is required for its binding to CRM1 and nuclear export. J. Biol. Chem. 277, 14355-14358
    • (2002) J. Biol. Chem. , vol.277 , pp. 14355-14358
    • Ishida, N.1    Hara, T.2    Kamura, T.3    Yoshida, M.4    Nakayama, K.5    Nakayama, K.I.6
  • 23
    • 0030848702 scopus 로고    scopus 로고
    • Catalytic properties of 26 S and 20 S proteasomes and radiolabeling of MB1, LMP7, and C7 subunits associated with trypsin-like and chymotrypsin-like activities
    • Reidlinger, J., Pike, A. M., Savory, P. J., Murray, R. Z., and Rivett, A. J. (1997) Catalytic properties of 26 S and 20 S proteasomes and radiolabeling of MB1, LMP7, and C7 subunits associated with trypsin-like and chymotrypsin-like activities. J. Biol. Chem. 272, 24899-24905
    • (1997) J. Biol. Chem. , vol.272 , pp. 24899-24905
    • Reidlinger, J.1    Pike, A.M.2    Savory, P.J.3    Murray, R.Z.4    Rivett, A.J.5
  • 24
    • 0029664461 scopus 로고    scopus 로고
    • Requirement of p27Kip1 for restriction point control of the fibroblast cell cycle
    • Coats, S., Flanagan, W. M., Nourse, J., and Roberts, J. M. (1996) Requirement of p27Kip1 for restriction point control of the fibroblast cell cycle. Science 272, 877-880
    • (1996) Science , vol.272 , pp. 877-880
    • Coats, S.1    Flanagan, W.M.2    Nourse, J.3    Roberts, J.M.4
  • 25
    • 0029979079 scopus 로고    scopus 로고
    • Inconstant association between 27-kDa heat shock protein (Hsp27) content and doxorubicin resistance in human colon cancer cells. The doxorubicin- protecting effect of Hsp27
    • Garrido, C., Mehlen, P., Fromentin, A., Hammann, A., Assem, M., Arrigo, A. P., and Chauffert, B. (1996) Inconstant association between 27-kDa heat shock protein (Hsp27) content and doxorubicin resistance in human colon cancer cells. The doxorubicin-protecting effect of Hsp27. Eur. J. Biochem. 237, 653-659
    • (1996) Eur. J. Biochem. , vol.237 , pp. 653-659
    • Garrido, C.1    Mehlen, P.2    Fromentin, A.3    Hammann, A.4    Assem, M.5    Arrigo, A.P.6    Chauffert, B.7
  • 26
    • 0036092428 scopus 로고    scopus 로고
    • Size matters: Of the small HSP27 and its large oligomers
    • Garrido, C. (2002) Size matters: of the small HSP27 and its large oligomers. Cell Death Differ. 9, 483-485
    • (2002) Cell Death Differ. , vol.9 , pp. 483-485
    • Garrido, C.1
  • 27
    • 0007404243 scopus 로고    scopus 로고
    • Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFalpha in NIH-3T3-ras cells
    • Mehlen, P., Hickey, E., Weber, L. A., and Arrigo, A. P. (1997) Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFalpha in NIH-3T3-ras cells. Biochem. Biophys. Res. Commun. 241, 187-192
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 187-192
    • Mehlen, P.1    Hickey, E.2    Weber, L.A.3    Arrigo, A.P.4
  • 29
    • 0028263008 scopus 로고
    • The serum-induced phosphorylation of mammalian hsp27 correlates with changes in its intracellular localization and levels of oligomerization
    • Mehlen, P., and Arrigo, A. P. (1994) The serum-induced phosphorylation of mammalian hsp27 correlates with changes in its intracellular localization and levels of oligomerization. Eur. J. Biochem. 221, 327-334
    • (1994) Eur. J. Biochem. , vol.221 , pp. 327-334
    • Mehlen, P.1    Arrigo, A.P.2
  • 30
    • 0042025074 scopus 로고    scopus 로고
    • Increased ubiquitin-dependent degradation can replace the essential requirement for heat shock protein induction
    • Friant, S., Meier, K. D., and Riezman, H. (2003) Increased ubiquitin-dependent degradation can replace the essential requirement for heat shock protein induction. EMBO J. 22, 3783-3791
    • (2003) EMBO J. , vol.22 , pp. 3783-3791
    • Friant, S.1    Meier, K.D.2    Riezman, H.3
  • 31
    • 0037974661 scopus 로고    scopus 로고
    • A role of HSPs in apoptosis through "protein triage"?
    • Garrido, C., and Solary, E. (2003) A role of HSPs in apoptosis through "protein triage"? Cell Death Differ. 10, 619-620
    • (2003) Cell Death Differ. , vol.10 , pp. 619-620
    • Garrido, C.1    Solary, E.2
  • 32
    • 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., Yew, P. R., Draetta, G. F., and Rolfe, M. (1995) Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27. Science 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    Yew, P.R.7    Draetta, G.F.8    Rolfe, M.9
  • 34
    • 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
  • 35
    • 0034682818 scopus 로고    scopus 로고
    • Phosphorylation at serine 10, a major phosphorylation site of p27(Kip1), increases its protein stability
    • Ishida, N., Kitagawa, M., Hatakeyama, S., and Nakayama, K. (2000) Phosphorylation at serine 10, a major phosphorylation site of p27(Kip1), increases its protein stability. J. Biol. Chem. 275, 25146-25154
    • (2000) J. Biol. Chem. , vol.275 , pp. 25146-25154
    • Ishida, N.1    Kitagawa, M.2    Hatakeyama, S.3    Nakayama, K.4
  • 36
    • 0035143141 scopus 로고    scopus 로고
    • Promotion of S-phase entry and cell growth under serum starvation by SAG/ROC2/Rbx2/Hrt2, an E3 ubiquitin ligase component: Association with inhibition of p27 accumulation
    • Duan, H., Tsvetkov, L. M., Liu, Y., Song, Y., Swaroop, M., Wen, R., Kung, H. F., Zhang, H., and Sun, Y. (2001) Promotion of S-phase entry and cell growth under serum starvation by SAG/ROC2/Rbx2/Hrt2, an E3 ubiquitin ligase component: association with inhibition of p27 accumulation. Mol. Carcinog. 30, 37-46
    • (2001) Mol. Carcinog. , vol.30 , pp. 37-46
    • Duan, H.1    Tsvetkov, L.M.2    Liu, Y.3    Song, Y.4    Swaroop, M.5    Wen, R.6    Kung, H.F.7    Zhang, H.8    Sun, Y.9
  • 37
    • 2342477917 scopus 로고    scopus 로고
    • The novel functions of ubiquitination in signaling
    • Sun, L., and Chen, Z. J. (2004) The novel functions of ubiquitination in signaling. Curr. Opin. Cell Biol. 16, 119-126
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 119-126
    • Sun, L.1    Chen, Z.J.2
  • 39
    • 4944252223 scopus 로고    scopus 로고
    • An Rb-Skp2-p27 pathway mediates acute cell cycle inhibition by Rb and is retained in a partial-penetrance Rb mutant
    • Ji, P., Jiang, H., Rekhtman, K., Bloom, J., Ichetovkin, M., Pagano, M., and Zhu, L. (2004) An Rb-Skp2-p27 pathway mediates acute cell cycle inhibition by Rb and is retained in a partial-penetrance Rb mutant. Mol. Cell 16, 47-58
    • (2004) Mol. Cell , vol.16 , pp. 47-58
    • Ji, P.1    Jiang, H.2    Rekhtman, K.3    Bloom, J.4    Ichetovkin, M.5    Pagano, M.6    Zhu, L.7
  • 40
    • 10344243550 scopus 로고    scopus 로고
    • Tuberin Binds p27 and Negatively Regulates Its Interaction with the SCF Component Skp2
    • Rosner, M., and Hengstschlager, M. (2004) Tuberin Binds p27 and Negatively Regulates Its Interaction with the SCF Component Skp2. J. Biol. Chem. 279, 48707-48715
    • (2004) J. Biol. Chem. , vol.279 , pp. 48707-48715
    • Rosner, M.1    Hengstschlager, M.2
  • 41
    • 0037648469 scopus 로고    scopus 로고
    • The small heat shock protein alpha B-crystallin promotes FBX4-dependent ubiquitination
    • den Engelsman, J., Keijsers, V., de Jong, W. W., and Boelens, W. C. (2003) The small heat shock protein alpha B-crystallin promotes FBX4-dependent ubiquitination. J. Biol. Chem. 278, 4699-4704
    • (2003) J. Biol. Chem. , vol.278 , pp. 4699-4704
    • Den Engelsman, J.1    Keijsers, V.2    De Jong, W.W.3    Boelens, W.C.4
  • 42
    • 0027366354 scopus 로고
    • The small heat shock protein hsp27 is correlated with growth and drug resistance in human breast cancer cell lines
    • Oesterreich, S., Weng, C. N., Qiu, M., Hilsenbeck, S. G., Osborne, C. K., and Fuqua, S. A. (1993) The small heat shock protein hsp27 is correlated with growth and drug resistance in human breast cancer cell lines. Cancer Res. 53, 4443-4448
    • (1993) Cancer Res. , vol.53 , pp. 4443-4448
    • Oesterreich, S.1    Weng, C.N.2    Qiu, M.3    Hilsenbeck, S.G.4    Osborne, C.K.5    Fuqua, S.A.6
  • 43
    • 0028919627 scopus 로고
    • Spontaneous overexpression of heat shock proteins in Ehrlich ascites carcinoma cells during in vivo growth
    • Gabai, V. L., Mosina, V. A., Budagova, K. R., and Kabakov, A. E. (1995) Spontaneous overexpression of heat shock proteins in Ehrlich ascites carcinoma cells during in vivo growth. Biochem. Mol. Biol. Int. 35, 95-102
    • (1995) Biochem. Mol. Biol. Int. , vol.35 , pp. 95-102
    • Gabai, V.L.1    Mosina, V.A.2    Budagova, K.R.3    Kabakov, A.E.4
  • 44
    • 0030785821 scopus 로고    scopus 로고
    • HSP27 as a mediator of confluence-dependent resistance to cell death induced by anticancer drugs
    • Garrido, C., Ottavi, P., Fromentin, A., Hammann, A., Arrigo, A. P., Chauffert, B., and Mehlen, P. (1997) HSP27 as a mediator of confluence-dependent resistance to cell death induced by anticancer drugs. Cancer Res. 57, 2661-2667
    • (1997) Cancer Res. , vol.57 , pp. 2661-2667
    • Garrido, C.1    Ottavi, P.2    Fromentin, A.3    Hammann, A.4    Arrigo, A.P.5    Chauffert, B.6    Mehlen, P.7
  • 45
    • 0037325853 scopus 로고    scopus 로고
    • Deregulated degradation of the cdk inhibitor p27 and malignant transformation
    • Bloom, J., and Pagano, M. (2003) Deregulated degradation of the cdk inhibitor p27 and malignant transformation. Semin. Cancer Biol. 13, 41-47
    • (2003) Semin. Cancer Biol. , vol.13 , pp. 41-47
    • Bloom, J.1    Pagano, M.2
  • 47
    • 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., Horii, I., and Loh, D. Y. (1996) Mice lacking p27(Kip1) display increased body size, multiple organ hyperplasia, retinal dysplasia, and pituitary tumors. Cell 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    Horii, I.7    Loh, D.Y.8
  • 49
    • 0032511848 scopus 로고    scopus 로고
    • The murine gene p27Kip1 is haplo-insufficient for tumour suppression
    • Fero, M. L., Randel, E., Gurley, K. E., Roberts, J. M., and Kemp, C. J. (1998) The murine gene p27Kip1 is haplo-insufficient for tumour suppression. Nature 396, 177-180
    • (1998) Nature , vol.396 , pp. 177-180
    • Fero, M.L.1    Randel, E.2    Gurley, K.E.3    Roberts, J.M.4    Kemp, C.J.5
  • 50
    • 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
  • 52
    • 0032054581 scopus 로고    scopus 로고
    • Heat shock protein 27: An independent prognostic indicator of survival in patients with epithelial ovarian carcinoma
    • Geisler, J. P., Geisler, H. E., Tammela, J., Wiemann, M. C., Zhou, Z., Miller, G. A., and Crabtree, W. (1998) Heat shock protein 27: an independent prognostic indicator of survival in patients with epithelial ovarian carcinoma. Gynecol. Oncol. 69, 14-16
    • (1998) Gynecol. Oncol. , vol.69 , pp. 14-16
    • Geisler, J.P.1    Geisler, H.E.2    Tammela, J.3    Wiemann, M.C.4    Zhou, Z.5    Miller, G.A.6    Crabtree, W.7
  • 53
    • 0036511128 scopus 로고    scopus 로고
    • Prognostic significance of heat shock protein 27 (HSP27) in patients with oral squamous cell carcinoma
    • Mese, H., Sasaki, A., Nakayama, S., Yoshioka, N., Yoshihama, Y., Kishimoto, K., and Matsumura, T. (2002) Prognostic significance of heat shock protein 27 (HSP27) in patients with oral squamous cell carcinoma. Oncol. Rep. 9, 341-344
    • (2002) Oncol. Rep. , vol.9 , pp. 341-344
    • Mese, H.1    Sasaki, A.2    Nakayama, S.3    Yoshioka, N.4    Yoshihama, Y.5    Kishimoto, K.6    Matsumura, T.7
  • 55
    • 0034081704 scopus 로고    scopus 로고
    • Hsp as novel regulators of programmed cell death and tumorigenicity
    • Arrigo, A. P. (2000) sHsp as novel regulators of programmed cell death and tumorigenicity. Pathol. Biol. (Paris) 48, 280-288
    • (2000) Pathol. Biol. (Paris) , vol.48 , pp. 280-288
    • Arrigo, A.P.1


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