210
Views
17
CrossRef citations to date
0
Altmetric
Research Article

Ubiquitination of heat shock protein 27 is mediated by its interaction with Smad ubiquitination regulatory factor 2 in A549 cells

, , , , , , & show all
Pages 568-573 | Received 10 Jun 2011, Accepted 30 Aug 2011, Published online: 03 Oct 2011

REFERENCES

  • Hershko A, Ciechanover A: The ubiquitin system. Annu Rev Biochem. 1998;67:425–479.
  • Pickart CM: Mechanisms underlying ubiquitination. Annu Rev Biochem. 2001;70:503–533.
  • Finley D, Ciechanover A, Varshavsky A: Ubiquitin as a central cellular regulator. Cell. 2004;116(Suppl 2):S29–S32, 2 pages following S32.
  • Hoeller D, Hecker CM, Dikic I: Ubiquitin and ubiquitin-like proteins in cancer pathogenesis. Nat Rev Cancer. 2006;6:776–788.
  • Zhang Y, Chang C, Gehling DJ, : Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase. Proc Natl Acad Sci U S A. 2001;98:974–979.
  • Richter K, Haslbeck M, Buchner J: The heat shock response: life on the verge of death. Mol Cell. 2010;40:253–266.
  • Lanneau D, Wettstein G, Bonniaud P, Garrido C: Heat shock proteins: cell protection through protein triage. Sci World J. 2010;10:1543–1052.
  • Khalil AA, Kabapy NF, Deraz SF, Smith C: Heat shock proteins in oncology: Diagnostic biomarkers or therapeutic targets? Biochim Biophys Acta. 2011;1816(2):89–104.
  • Gonzalez-Mejia ME, Voss OH, Murnan EJ, Doseff AI: Apigenin-induced apoptosis of leukemia cells is mediated by a bimodal and differentially regulated residue-specific phosphorylation of heat-shock protein-27. Cell Death Dis. 2010;1(8): e64.
  • Concannon CG, Gorman AM, Samali A: On the role of Hsp27 in regulating apoptosis. Apoptosis. 2003;8:61–70.
  • Neutzner A, Benard G, Youle RJ, Karbowski M: Role of the ubiquitin conjugation system in the maintenance of mitochondrial homeostasis. Ann N Y Acad Sci. 2008;1147:242–253.
  • Nakayama KI, Nakayama K: Ubiquitin ligases: cell-cycle control and cancer. Nat Rev Cancer. 2006;6:369–381.
  • Zhang Y, Chang C, Gehling DJ, : Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase. Proc Natl Acad Sci U S A. 2001;98:974–979.
  • Ogunjimi AA, Briant DJ, Pece-Barbara N, : Regulation of Smurf2 ubiquitin ligase activity by anchoring the E2 to the HECT domain. Mol Cell. 2005;19:297–308.
  • Lönn P, Morén A, Raja E, : Regulating the stability of TGF beta receptors and Smads. Cell Res. 2009;19:21–35.
  • Kavsak P, Rasmussen RK, Causing CG, : Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation. Mol Cell. 2000;6:1365–1375.
  • Garrido C, Schmitt E, Candé C, Vahsen N, Parcellier A, Kroemer G: HSP27 and HSP70: potentially oncogenic apoptosis inhibitors. Cell Cycle. 2003;2:579–84.
  • Langmár Z, Vleskó G: The potential role of heat shock proteins in the treatment of ovarian cancer. Orv Hetil. 2011;152: 92–95.
  • Eskenazi AE, Powers J, Pinkas J, Oesterreich S, Fuqua SA, Frantz CN: Induction of heat shock protein 27 by hydroxyurea and its relationship to experimental metastasis. Clin Exp Metastasis. 1998;16:283–290.
  • Casas A, Di Venosa G, Hasan T, Al Batlle: Mechanisms of resistance to photodynamic therapy. Curr Med Chem. 2011;18:2486–515.
  • Hsu HS, Lin JH, Huang WC, : Chemoresistance of lung cancer stemlike cells depends on activation of Hsp27. Cancer. 2011;117:1516–1528.
  • Choi SH, Lee YJ, Seo WD, : Altered cross-linking of HSP27 by zerumbone as a novel strategy for overcoming HSP27-mediated radioresistance. Int J Radiat Oncol Biol Phys. 2011;79:1196–1205.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.