The deubiquitinase USP10 protects pancreatic cancer cells from endoplasmic reticulum stress

被引：5

作者：

Bhattacharya, Udayan ^{[1
]}

Thavathiru, Elangovan ^{[1
]}

Neizer-Ashun, Fiifi ^{[2
]}

Xu, Chao ^{[3
]}

Gatalica, Zoran ^{[4
]}

Dwivedi, Shailendra Kumar Dhar ^{[1
]}

Dey, Anindya ^{[1
]}

Mukherjee, Priyabrata ^{[4
,5
]}

Bhattacharya, Resham ^{[1
,2
,4
,5
]}

机构：

[1] Univ Oklahoma, Dept Obstet & Gynecol, Hlth Sci Ctr, Oklahoma City, OK 73117 USA

[2] Univ Oklahoma, Dept Cell Biol, Hlth Sci Ctr, Oklahoma City, OK 73117 USA

[3] Univ Oklahoma, Dept Biostat & Epidemiol, Hlth Sci Ctr, Oklahoma City, OK USA

[4] Univ Oklahoma, Dept Pathol, Hlth Sci Ctr, Oklahoma City, OK 73117 USA

[5] Univ Oklahoma, Peggy & Charles Stephenson Canc Ctr, Hlth Sci Ctr, Oklahoma City, OK 73117 USA

来源：

NPJ PRECISION ONCOLOGY | 2022年 / 6卷 / 01期

基金：

美国国家卫生研究院;

关键词：

ACTIVATION; COMPLEX;

D O I：

10.1038/s41698-022-00336-x

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

The ubiquitin-specific peptidase 10 (USP10) plays a context-specific, pro or anti-tumorigenic role in different malignancies. However, the role of USP10 in pancreatic cancer remains unclear. Our protein and RNA level analysis from archived specimens and public databases show that USP10 is overexpressed in pancreatic ductal adenocarcinoma (PDAC) and expression correlates with poor overall patient survival. Phenotypically, silencing USP10 decreased viability, clonal growth and invasive properties of pancreatic cancer cells. Mechanistically, silencing USP10 upregulated BiP and induced endoplasmic reticulum (ER) stress that led to an unfolded protein response (UPR) and upregulation of PERK, IRE1 alpha. Decreased cell viability of USP10 silenced cells could be rescued by a chemical chaperone that promotes protein folding. Our studies suggest that USP10 by protecting pancreatic cancer cells from ER stress may support tumor progression.

引用

页数：6

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