Major heat shock protein Hsp72 controls oncogene-induced senescence.
Various heat shock proteins, including Hsp72, are strongly upregulated in cancers, but their significance for tumor emergence and growth is poorly understood. Here we review recent data from several labs to indicate that Hsps, including Hsp72, are critical for growth of transformed but not normal cells. By manipulating expression and activity of Hsp72 and several oncogenes, it was shown that Hsp72 suppresses oncogene-induced senescence, thus allowing proliferation of cancer cells. Importantly, Hsp72 is able to suppress both p53-dependent and p53-independent senescence pathways. We propose that targeting Hsp72 may be a promising approach toward development of novel cancer therapies.
Department of Biochemistry, Boston University Medical School, Boston, Massachusetts, USA. sherma1@bu.edu
Michael
M
Sherman
D000375:Aging / Q000235:genetics*; D050884:HSP72 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D009369:Neoplasms / Q000235:genetics / Q000473:pathology; D009857:Oncogenes; D016159:Tumor Suppressor Protein p53 / Q000235:genetics / Q000378:metabolism*
D050884:HSP72 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D016159:Tumor Suppressor Protein p53