Structure and function of the co-chaperone protein phosphatase 5 in cancer

被引：28
|
作者：
Sager, Rebecca A. [1 ,2 ,3 ,4 ]
Dushukyan, Natela [1 ,2 ,3 ]
Woodford, Mark [1 ,2 ,3 ]
Mollapour, Mehdi [1 ,2 ,3 ]
机构：
[1] SUNY Upstate Med Univ, Dept Urol, Syracuse, NY 13210 USA
[2] SUNY Upstate Med Univ, Dept Biochem & Mol Biol, Syracuse, NY 13210 USA
[3] SUNY Upstate Med Univ, Upstate Canc Ctr, Syracuse, NY 13210 USA
[4] SUNY Upstate Med Univ, Coll Med, Syracuse, NY 13210 USA
来源：
CELL STRESS & CHAPERONES | 2020年 / 25卷 / 03期
关键词：
Serine; threonine phosphatase 5; Molecular chaperone; Co-chaperone; Heat shock protein 90; Clear cell renal cell carcinoma; Cancer; Post-translational modifications; GLUCOCORTICOID-RECEPTOR PHOSPHORYLATION; TETRATRICOPEPTIDE REPEAT; MOLECULAR CHAPERONE; SERINE/THREONINE PHOSPHATASES; POSTTRANSLATIONAL REGULATION; HEPATOCELLULAR-CARCINOMA; ALPHA PHOSPHORYLATION; FEEDBACK-REGULATION; NEGATIVE REGULATOR; S100; PROTEINS;
D O I：
10.1007/s12192-020-01091-3
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
Protein phosphatase 5 (PP5) is a serine/threonine protein phosphatase that regulates many cellular functions including steroid hormone signaling, stress response, proliferation, apoptosis, and DNA repair. PP5 is also a co-chaperone of the heat shock protein 90 molecular chaperone machinery that assists in regulation of cellular signaling pathways essential for cell survival and growth. PP5 plays a significant role in survival and propagation of multiple cancers, which makes it a promising target for cancer therapy. Though there are several naturally occurring PP5 inhibitors, none is specific for PP5. Here, we review the roles of PP5 in cancer progression and survival and discuss the unique features of the PP5 structure that differentiate it from other phosphoprotein phosphatase (PPP) family members and make it an attractive therapeutic target.
引用
收藏
页码：383 / 394
页数：12
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