Molecular chaperones regulate p53 and suppress senescence programs

被引:36
作者
Sherman, Michael [1 ]
Gabai, Vladimir [1 ]
O'Callaghan, Cornelia [1 ]
Yaglom, Julia [1 ]
机构
[1] Boston Univ, Sch Med, Dept Biochem, Boston, MA 02118 USA
关键词
heat shock proteins; mortalin; hsp70; senescence; p21; p53; cancer;
D O I
10.1016/j.febslet.2007.05.036
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Many types of cancer cells constitutively express major molecular chaperones at high levels. Recent findings demonstrate that specific depletion of individual chaperones, including various members of the Hsp70 family, small heat shock proteins, or VCP/p97, leads to activation of p53 pathway and subsequently triggers cellular senescence. Here, we discuss a possibility that in cancer cells high levels of chaperones serve to keep the p53 signaling under control, thus allowing cancer cells to evade the default senescence and form tumors. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:3711 / 3715
页数:5
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