Proteasomal deubiquitinase UCH37 inhibits degradation of β-catenin and promotes cell prol

Proteasomal deubiquitinase UCH37 inhibits degradation of β-catenin and promotes cell

proliferation and motility

Zijian Li;Luming Zhou;Tianxia Jiang;Libin Fan;Xiaoying Liu;Xiaobo Qiu

【期刊名称】《生物化学与生物物理学报：英文版》 【年(卷),期】2019(051)003

【摘要】The ubiquitin-proteasome system degrades most cellular proteins in eukaryotes.UCH37,also known as UCH-L5,is a deubiquitinase binding to Rpn13,a receptor for ubiquitinated substrates in the 26 S proteasome.But,it remains unclear how UCH37 influences the proteasomal degradation of the ubiquitinated substrates.Because deletion of UCH37 is embryonically lethal in mice,this study aims to investigate the role of UCH37 in proteasomal degradation by constructing the UCH37-deficient cell lines using CRISPR/Cas9 technology.Our results demonstrated that deletion of UCH37decreased the levels of proteasomal Rpn13,implying that UCH37 might facilitate incorporation of Rpn13 into the proteasome.Meanwhile,deletion of UCH37 decreased the levels of β-catenin and the early endosomal protein

Rab8.β-Catenin

interacts

with

TCF/LEF

to

control

transcription,and is involved in development,tissue homeostasis and tumorigenesis.We further found that deletion of UCH37 increased the levels of the ubiquitinated β-catenin and accelerated the hydrogen