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Volumn 287, Issue 52, 2012, Pages 43639-43650

The mRNA-stabilizing factor HuR protein is targeted by β-TrCP protein for degradation in response to glycolysis inhibition

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE SUBSTITUTION; CANCER CELLS; CANCER THERAPY; CO-IMMUNOPRECIPITATIONS; CYTOPLASMIC LOCALIZATION; DEGRADATION PATHWAYS; DIVERSE STRESS; DOMINANT NEGATIVE; E3 LIGASE; GLUCOSE TRANSPORTERS; GST PULL-DOWN; HEAT-SHOCK; IN-VITRO; MECHANISTIC LINK; METABOLIC STRESS; MUTATIONAL ANALYSIS; NOVEL STRATEGIES; NUCLEAR EXPORT; ONCOGENIC PROTEINS; POST-TRANSLATIONAL MODIFICATIONS; PROTEASOMAL DEGRADATION; PROTECTIVE EFFECTS; PROTEIN STABILITY; RECOGNITION SITE; RNA-RECOGNITION MOTIFS; STRESS RESPONSE PROTEINS; STRESS STIMULUS; UBIQUITIN; UBIQUITINATION;

EID: 84871589889     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.393678     Document Type: Article
Times cited : (47)

References (36)
  • 1
    • 84860332384 scopus 로고    scopus 로고
    • HuR function in disease
    • Srikantan, S., and Gorospe, M. (2012) HuR function in disease. Front. Biosci. 17, 189-205
    • (2012) Front. Biosci. , vol.17 , pp. 189-205
    • Srikantan, S.1    Gorospe, M.2
  • 2
    • 79952759375 scopus 로고    scopus 로고
    • Posttranscriptional regulation of cancer traits by HuR
    • Abdelmohsen, K., and Gorospe, M. (2010) Posttranscriptional regulation of cancer traits by HuR. Wiley Interdiscip. Rev. RNA 1, 214-229
    • (2010) Wiley Interdiscip. Rev. RNA , vol.1 , pp. 214-229
    • Abdelmohsen, K.1    Gorospe, M.2
  • 3
    • 53849124668 scopus 로고    scopus 로고
    • Diverse molecular functions of Hu proteins
    • Hinman, M. N., and Lou, H. (2008) Diverse molecular functions of Hu proteins. Cell Mol. Life Sci. 65, 3168-3181
    • (2008) Cell Mol. Life Sci. , vol.65 , pp. 3168-3181
    • Hinman, M.N.1    Lou, H.2
  • 4
    • 23344431879 scopus 로고    scopus 로고
    • Delayed mechanism for induction of γ-glutamylcysteine synthetase heavy subunit mRNA stability by oxidative stress involving p38 mitogen-activated protein kinase signaling
    • DOI 10.1074/jbc.M413103200
    • Song, I. S., Tatebe, S., Dai, W., and Kuo, M. T. (2005) Delayed mechanism for induction of γ-glutamylcysteine synthetase heavy subunit mRNA stability by oxidative stress involving p38 mitogen-activated protein kinase signaling. J. Biol. Chem. 280, 28230-28240 (Pubitemid 41105719)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.31 , pp. 28230-28240
    • Song, I.-S.1    Tatebe, S.2    Dai, W.3    Kuo, M.T.4
  • 6
    • 80052741232 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of RNA-binding protein HuR regulates c-Myc protein expression after hypoxic stress
    • Talwar, S., Jin, J., Carroll, B., Liu, A., Gillespie, M. B., and Palanisamy, V. (2011) Caspase-mediated cleavage of RNA-binding protein HuR regulates c-Myc protein expression after hypoxic stress. J. Biol. Chem. 286, 32333-32343
    • (2011) J. Biol. Chem. , vol.286 , pp. 32333-32343
    • Talwar, S.1    Jin, J.2    Carroll, B.3    Liu, A.4    Gillespie, M.B.5    Palanisamy, V.6
  • 8
  • 10
    • 0036787920 scopus 로고    scopus 로고
    • Highly selective actions of HuR in antagonizing AU-rich element-mediated mRNA destabilization
    • Chen, C. Y., Xu, N., and Shyu, A. B. (2002) Highly selective actions of HuR in antagonizing AU-rich element-mediated mRNA destabilization. Mol. Cell Biol. 22, 7268-7278
    • (2002) Mol. Cell Biol. , vol.22 , pp. 7268-7278
    • Chen, C.Y.1    Xu, N.2    Shyu, A.B.3
  • 12
    • 33747601610 scopus 로고    scopus 로고
    • Expression of the ELAV-like protein HuR in human colon cancer: Association with tumor stage and cyclooxygenase-2
    • DOI 10.1038/modpathol.3800645, PII 3800645
    • Denkert, C., Koch, I., von Keyserlingk, N., Noske, A., Niesporek, S., Dietel, M., and Weichert, W. (2006) Expression of the ELAV-like protein HuR in human colon cancer: association with tumor stage and cyclooxygenase-2. Mod. Pathol. 19, 1261-1269 (Pubitemid 44268197)
    • (2006) Modern Pathology , vol.19 , Issue.9 , pp. 1261-1269
    • Denkert, C.1    Koch, I.2    Von Keyserlingk, N.3    Noske, A.4    Niesporek, S.5    Dietel, M.6    Weichert, W.7
  • 13
    • 0345707583 scopus 로고    scopus 로고
    • Cytoplasmic HuR Expression Correlates with Poor Outcome and with Cyclooxygenase 2 Expression in Serous Ovarian Carcinoma
    • Erkinheimo, T. L., Lassus, H., Sivula, A., Sengupta, S., Furneaux, H., Hla, T., Haglund, C., Butzow, R., and Ristimäki, A. (2003) Cytoplasmic HuR expression correlates with poor outcome and with cyclooxygenase 2 expression in serous ovarian carcinoma. Cancer Res. 63, 7591-7594 (Pubitemid 37466678)
    • (2003) Cancer Research , vol.63 , Issue.22 , pp. 7591-7594
    • Erkinheimo, T.-L.1    Lassus, H.2    Sivula, A.3    Sengupta, S.4    Furneaux, H.5    Hla, T.6    Haglund, C.7    Butzow, R.8    Ristimaki, A.9
  • 16
    • 58149511991 scopus 로고    scopus 로고
    • MiR-519 reduces cell proliferation by lowering RNA-binding protein HuR levels
    • Abdelmohsen, K., Srikantan, S., Kuwano, Y., and Gorospe, M. (2008) miR-519 reduces cell proliferation by lowering RNA-binding protein HuR levels. Proc. Natl. Acad. Sci. U.S.A. 105, 20297-20302
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 20297-20302
    • Abdelmohsen, K.1    Srikantan, S.2    Kuwano, Y.3    Gorospe, M.4
  • 17
    • 77950584927 scopus 로고    scopus 로고
    • MicroRNA-125a represses cell growth by targeting HuR in breast cancer
    • Guo, X., Wu, Y., and Hartley, R. S. (2009) MicroRNA-125a represses cell growth by targeting HuR in breast cancer. RNA Biol. 6, 575-583
    • (2009) RNA Biol. , vol.6 , pp. 575-583
    • Guo, X.1    Wu, Y.2    Hartley, R.S.3
  • 20
    • 55549109429 scopus 로고    scopus 로고
    • A novel mechanism by which thiazolidinediones facilitate the proteasomal degradation of cyclin D1 in cancer cells
    • Wei, S., Yang, H. C., Chuang, H. C., Yang, J., Kulp, S. K., Lu, P. J., Lai, M. D., and Chen, C. S. (2008) A novel mechanism by which thiazolidinediones facilitate the proteasomal degradation of cyclin D1 in cancer cells. J. Biol. Chem. 283, 26759-26770
    • (2008) J. Biol. Chem. , vol.283 , pp. 26759-26770
    • Wei, S.1    Yang, H.C.2    Chuang, H.C.3    Yang, J.4    Kulp, S.K.5    Lu, P.J.6    Lai, M.D.7    Chen, C.S.8
  • 21
    • 77951242981 scopus 로고    scopus 로고
    • Energy restriction as an antitumor target of thiazolidinediones
    • Wei, S., Kulp, S. K., and Chen, C. S. (2010) Energy restriction as an antitumor target of thiazolidinediones. J. Biol. Chem. 285, 9780-9791
    • (2010) J. Biol. Chem. , vol.285 , pp. 9780-9791
    • Wei, S.1    Kulp, S.K.2    Chen, C.S.3
  • 22
    • 84867432711 scopus 로고    scopus 로고
    • Targeting the oncogenic e3 ligase skp2 in prostate and breast cancer cells with a novel energy restriction-mimetic agent
    • Wei, S., Chu, P. C., Chuang, H. C., Hung, W. C., Kulp, S. K., and Chen, C. S. (2012) Targeting the oncogenic e3 ligase skp2 in prostate and breast cancer cells with a novel energy restriction-mimetic agent. PLoS ONE 7, e47298
    • (2012) PLoS ONE , vol.7
    • Wei, S.1    Chu, P.C.2    Chuang, H.C.3    Hung, W.C.4    Kulp, S.K.5    Chen, C.S.6
  • 24
    • 0033611567 scopus 로고    scopus 로고
    • The human F box protein β-Trcp associates with the Cul1/Skp1 complex and regulates the stability of β-catenin
    • DOI 10.1038/sj.onc.1202653
    • Latres, E., Chiaur, D. S., and Pagano, M. (1999) The human F box protein β-Trcp associates with the Cul1/Skp1 complex and regulates the stability of β-catenin. Oncogene 18, 849-854 (Pubitemid 29086261)
    • (1999) Oncogene , vol.18 , Issue.4 , pp. 849-854
    • Latres, E.1    Chiaur, D.S.2    Pagano, M.3
  • 26
    • 34250362729 scopus 로고    scopus 로고
    • Protein kinase Cα-dependent phosphorylation of the mRNA-stabilizing factor HuR: Implications for posttranscriptional regulation of cyclooxygenase-2
    • DOI 10.1091/mbc.E06-09-0850
    • Doller, A., Huwiler, A., Müller, R., Radeke, H. H., Pfeilschifter, J., and Eberhardt, W. (2007) Protein kinase C α-dependent phosphorylation of the mRNA-stabilizing factor HuR. Implications for posttranscriptional regulation of cyclooxygenase-2. Mol. Biol. Cell 18, 2137-2148 (Pubitemid 46911365)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.6 , pp. 2137-2148
    • Doller, A.1    Huwiler, A.2    Muller, R.3    Radeke, H.H.4    Pfeilschifter, J.5    Eberhardt, W.6
  • 27
    • 42149150455 scopus 로고    scopus 로고
    • Posttranslational modification of the AU-rich element binding protein HuR by protein kinase CΔ elicits angiotensin II-induced stabilization and nuclear export of cyclooxygenase 2 mRNA
    • Doller, A., Akool el-S, Huwiler, A., Müller, R., Radeke, H. H., Pfeilschifter, J., and Eberhardt, W. (2008) Posttranslational modification of the AU-rich element binding protein HuR by protein kinase CΔ elicits angiotensin II-induced stabilization and nuclear export of cyclooxygenase 2 mRNA. Mol. Cell Biol. 28, 2608-2625
    • (2008) Mol. Cell Biol. , vol.28 , pp. 2608-2625
    • Doller, A.1    Akool, El.-S.2    Huwiler, A.3    Müller, R.4    Radeke, H.H.5    Pfeilschifter, J.6    Eberhardt, W.7
  • 28
    • 55849099956 scopus 로고    scopus 로고
    • Modification at HuR(S242) alters HuR localization and proliferative influence
    • Kim, H. H., Yang, X., Kuwano, Y., and Gorospe, M. (2008) Modification at HuR(S242) alters HuR localization and proliferative influence. Cell Cycle 7, 3371-3377
    • (2008) Cell Cycle , vol.7 , pp. 3371-3377
    • Kim, H.H.1    Yang, X.2    Kuwano, Y.3    Gorospe, M.4
  • 29
    • 44349122993 scopus 로고    scopus 로고
    • Deregulated proteolysis by the F-box proteins SKP2 and β-TrCP: Tipping the scales of cancer
    • DOI 10.1038/nrc2396, PII NRC2396
    • Frescas, D., and Pagano, M. (2008) Deregulated proteolysis by the F-box proteins SKP2 and β-TrCP. Tipping the scales of cancer. Nat. Rev. Cancer 8, 438-449 (Pubitemid 351744963)
    • (2008) Nature Reviews Cancer , vol.8 , Issue.6 , pp. 438-449
    • Frescas, D.1    Pagano, M.2
  • 33
    • 80053986419 scopus 로고    scopus 로고
    • Regulation of HuR by DNA damage response kinases
    • pii: 981487
    • Kim, H. H., Abdelmohsen, K., and Gorospe, M. (2010) Regulation of HuR by DNA damage response kinases. J. Nucleic Acids 2010, pii: 981487
    • (2010) J. Nucleic Acids , vol.2010
    • Kim, H.H.1    Abdelmohsen, K.2    Gorospe, M.3
  • 34
    • 39149136475 scopus 로고    scopus 로고
    • ATM-dependent nuclear accumulation of IKK-α plays an important role in the regulation of p73-mediated apoptosis in response to cisplatin
    • DOI 10.1038/sj.onc.1210722, PII 1210722
    • Yoshida, K., Ozaki, T., Furuya, K., Nakanishi, M., Kikuchi, H., Yamamoto, H., Ono, S., Koda, T., Omura, K., and Nakagawara, A. (2008) ATM-dependent nuclear accumulation of IKK-α plays an important role in the regulation of p73-mediated apoptosis in response to cisplatin. Oncogene 27, 1183-1188 (Pubitemid 351253185)
    • (2008) Oncogene , vol.27 , Issue.8 , pp. 1183-1188
    • Yoshida, K.1    Ozaki, T.2    Furuya, K.3    Nakanishi, M.4    Kikuchi, H.5    Yamamoto, H.6    Ono, S.7    Koda, T.8    Omura, K.9    Nakagawara, A.10
  • 36
    • 73649138927 scopus 로고    scopus 로고
    • Chemical inhibitors destabilize HuR binding to the AU-rich element of TNF-α mRNA
    • Chae, M. J., Sung, H. Y., Kim, E. H., Lee, M., Kwak, H., Chae, C. H., Kim, S., and Park, W. Y. (2009) Chemical inhibitors destabilize HuR binding to the AU-rich element of TNF-α mRNA. Exp. Mol. Med. 41, 824-831
    • (2009) Exp. Mol. Med. , vol.41 , pp. 824-831
    • Chae, M.J.1    Sung, H.Y.2    Kim, E.H.3    Lee, M.4    Kwak, H.5    Chae, C.H.6    Kim, S.7    Park, W.Y.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.