The deubiquitinase USP38 affects cellular functions through interacting with LSD1

Biological research: BR

Qi Zhang¹  Yuanyuan Fang²  Wenbin Liu³ 

[1] College of Health Sciences and Nursing, Wuhan Polytechnic University, Wuhan, China;College of Life Sciences, Wuhan University, Wuhan, China;Hubei Key Laboratory of Animal Nutrition and Feed Science, Wuhan Polytechnic University, Wuhan, China

关键词: LSD1;    Deubiquitinase;    USP38;    Proliferation;   

DOI  :  10.1186/s40659-018-0201-8

学科分类：生物科学（综合）

来源: BioMed Central

【 摘 要 】

Deubiquitination is a posttranslational protein modification prevalent in mammalian cells. Deubiquitinases regulate the functions of the target protein by removing its ubiquitin chain. In this study, the effects of the deubiquitinase USP38’s functions on the LSD1 protein and on cell physiology were investigated. Western blotting, real-time quantitative PCR, immunoprecipitation, denaturing immunoprecipitation and luciferase reporter assays were used to analyze the protein stability, protein interactions and changes in the ubiquitin chain. Cell proliferation assays, colony formation assays, drug treatments and western blotting were used to explore the functions of USP38 in cells. The deubiquitinase USP38 stabilizes protein LSD1 in cells by binding LSD1 and cleaving its ubiquitin chain to prevent the degradation of LSD1 by the intracellular proteasome. USP38 enhances the ability of LSD1 to activate signaling pathways and hence promotes cellular abilities of proliferation and colony formation through interacting with LSD1. Furthermore, USP38 enhances the drug tolerance of human colon cancer cells. USP38 is an LSD1-specific deubiquitinase that affects cellular physiology through interacting with LSD1.

【 授权许可】

CC BY