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
相关论文
共 50 条
  • [41] The Plasticity of the Hsp90 Co-chaperone System
    Sahasrabudhe, Priyanka
    Rohrberg, Julia
    Biebl, Maximillian M.
    Rutz, Daniel A.
    Buchner, Johannes
    MOLECULAR CELL, 2017, 67 (06) : 947 - +
  • [42] The myosin co-chaperone UNC-45 is required for skeletal and cardiac muscle function in zebrafish
    Wohlgemuth, Serene L.
    Crawford, Bryan D.
    Pilgrim, David B.
    DEVELOPMENTAL BIOLOGY, 2007, 303 (02) : 483 - 492
  • [43] The FKBP51 Glucocorticoid Receptor Co-Chaperone: Regulation, Function, and Implications in Health and Disease
    Fries, Gabriel R.
    Gassen, Nils C.
    Rein, Theo
    INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2017, 18 (12)
  • [44] The p23 co-chaperone protein is a novel substrate of CK2 in Arabidopsis
    Kendra Tosoni
    Alex Costa
    Stefania Sarno
    Stefano D’Alessandro
    Francesca Sparla
    Lorenzo A. Pinna
    Michela Zottini
    Maria Ruzzene
    Molecular and Cellular Biochemistry, 2011, 356 : 245 - 254
  • [45] c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells
    Dunn, Diana M.
    Woodford, Mark R.
    Truman, Andrew W.
    Jensen, Sandra M.
    Schulman, Jacqualyn
    Caza, Tiffany
    Remillard, Taylor C.
    Loiselle, David
    Wolfgeher, Donald
    Blagg, Brian S. J.
    Franco, Lucas
    Haystead, Timothy A.
    Daturpalli, Soumya
    Mayer, Matthias P.
    Trepel, Jane B.
    Morgan, Rhodri M. L.
    Prodromou, Chrisostomos
    Kron, Stephen J.
    Panaretou, Barry
    Stetler-Stevenson, William G.
    Landas, Steve K.
    Neckers, Len
    Bratslavsky, Gennady
    Bourboulia, Dimitra
    Mollapour, Mehdi
    CELL REPORTS, 2015, 12 (06): : 1006 - 1018
  • [46] The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
    Patrice Connell
    Carol A. Ballinger
    Jihong Jiang
    Yaxu Wu
    Larry J. Thompson
    Jörg Höhfeld
    Cam Patterson
    Nature Cell Biology, 2001, 3 : 93 - 96
  • [47] The p23 co-chaperone protein is a novel substrate of CK2 in Arabidopsis
    Tosoni, Kendra
    Costa, Alex
    Sarno, Stefania
    D'Alessandro, Stefano
    Sparla, Francesca
    Pinna, Lorenzo A.
    Zottini, Michela
    Ruzzene, Maria
    MOLECULAR AND CELLULAR BIOCHEMISTRY, 2011, 356 (1-2) : 245 - 254
  • [48] Tic40, a membrane-anchored co-chaperone homolog in the chloroplast protein translocon
    Chou, ML
    Fitzpatrick, LM
    Tu, SL
    Budziszewski, G
    Potter-Lewis, S
    Akita, M
    Levin, JZ
    Keegstra, K
    Li, HM
    EMBO JOURNAL, 2003, 22 (12): : 2970 - 2980
  • [49] Polymorphisms in FKBP5, a co-chaperone of the glucocorticoid receptor are associated with response to antidepressant drugs
    Binder, EB
    Salyakina, D
    Wochnik, G
    Ising, M
    Pütz, B
    Kern, N
    Lucae, S
    Mueller, JC
    Lohmussaar, E
    Meitinger, T
    Baghai, T
    Bondy, B
    Rupprecht, R
    Uhr, M
    Rein, T
    Holsboer, F
    Müller-Myhsok, B
    AMERICAN JOURNAL OF MEDICAL GENETICS PART B-NEUROPSYCHIATRIC GENETICS, 2004, 130B (01) : 13 - 13
  • [50] Cloning, Expression and Crystallisation of SGT1 Co-chaperone Protein from Glaciozyma antarctica
    Yusof, Nur Athirah
    Abu Bakar, Farah Diba
    Beddoe, Travis
    Murad, Abdul Munir Abdul
    2013 UKM FST POSTGRADUATE COLLOQUIUM, 2013, 1571 : 292 - 297
12345