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Oncol Lett. 2015 Sep;10(3):1655-1661. doi: 10.3892/ol.2015.3406. Epub 2015 Jun 22.

Rheb phosphorylation is involved in p38-regulated/activated protein kinase-mediated tumor suppression in liver cancer.

Oncology letters

Min Zheng, Shengbing Zang, Linna Xie, Xueting Fang, Y U Zhang, Xiaojie Ma, Jingfeng Liu, Dexin Lin, Aimin Huang

Affiliations

  1. Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Fujian Medical University, Fuzhou, Fujian 350004, P.R. China ; Translational Medicine Institute, Fujian Medical University, Fuzhou, Fujian 350004, P.R. China.
  2. Department of Pathology and Institute of Oncology, School of Basic Medical Sciences, Fujian Medical University, Fuzhou, Fujian 350004, P.R. China.
  3. Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Fujian Medical University, Fuzhou, Fujian 350004, P.R. China ; Department of Bioengineering, Fujian Vocational College of Bioengineering, Fuzhou, Fujian 350007, P.R. China.
  4. Liver Center of Fujian Province, Mengchao Hepatobiliary Hospital of Fujian Medical University, Fuzhou, Fujian 350025, P.R. China.
  5. Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Fujian Medical University, Fuzhou, Fujian 350004, P.R. China.

PMID: 26622727 PMCID: PMC4533698 DOI: 10.3892/ol.2015.3406

Abstract

Ras homolog enriched in brain (Rheb) is a key regulator of mammalian target of rapamycin complex 1 (mTORC1). The Rheb-mTORC1 axis is a pivotal pathway that mediates cell growth. It was previously reported that upon energy-stress stimulation, the phosphorylation of Rheb at serine 130 by p38-regulated/activated protein kinase (PRAK) results in the impaired nucleotide binding ability of Rheb and inhibits Rheb-mediated mTORC1 activation. However, the role of Rheb phosphorylation in cancer development remains to be elucidated. The aim of the present study was to determine the effect of Rheb phosphorylation on tumor growth

Keywords: Ras; Rheb phosphorylation; liver cancer; p38-regulated/activated protein kinase

References

  1. Curr Drug Targets. 2011 Jul 1;12(8):1223-31 - PubMed
  2. Cancer. 1954 May;7(3):462-503 - PubMed
  3. Nat Cell Biol. 2011 Mar;13(3):263-72 - PubMed
  4. Cell. 1997 Mar 7;88(5):593-602 - PubMed
  5. Front Oncol. 2014 Sep 29;4:262 - PubMed
  6. Prostate. 2010 Jun 1;70(8):866-74 - PubMed
  7. Nature. 2006 May 25;441(7092):424-30 - PubMed
  8. Cancer Res. 2010 Apr 15;70(8):3287-98 - PubMed
  9. Oncol Rep. 2013 May;29(5):1969-74 - PubMed
  10. Anat Rec (Hoboken). 2009 Aug;292(8):1128-34 - PubMed
  11. J Biol Chem. 1994 Jun 10;269(23):16333-9 - PubMed
  12. Nat Cell Biol. 2007 May;9(5):483-5 - PubMed
  13. Cell. 2011 Mar 4;144(5):646-74 - PubMed
  14. Curr Cancer Drug Targets. 2010 Dec;10(8):869-76 - PubMed
  15. Curr Opin Cell Biol. 2008 Apr;20(2):150-5 - PubMed
  16. Oncol Lett. 2012 Nov;4(5):873-877 - PubMed
  17. Nature. 2005 Aug 4;436(7051):660-5 - PubMed
  18. Genes Dev. 2008 Aug 15;22(16):2172-7 - PubMed
  19. Nat Med. 1998 Jul;4(7):844-7 - PubMed
  20. Cell. 2007 Jan 26;128(2):295-308 - PubMed
  21. Biochem Soc Trans. 2012 Feb;40(1):139-46 - PubMed
  22. Genes Dev. 2003 Aug 1;17(15):1829-34 - PubMed
  23. Korean J Pathol. 2012 Aug;46(4):324-30 - PubMed
  24. J Natl Cancer Inst. 2008 May 21;100(10):698-711 - PubMed
  25. Cancer Lett. 2010 Nov 1;297(1):117-25 - PubMed
  26. Genes Dev. 2008 Aug 15;22(16):2178-88 - PubMed
  27. Mol Biol Cell. 2003 Jun;14(6):2603-16 - PubMed

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