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The deubiquitinase USP36 promotes snoRNP group SUMOylation and is essential for ribosome biogenesis
Author(s) -
Ryu Hyunju,
Sun XiaoXin,
Chen Yingxiao,
Li Yanping,
Wang Xiaoyan,
Dai Roselyn S,
Zhu HongMing,
Klimek John,
David Larry,
Fedorov Lev M,
Azuma Yoshiaki,
Sears Rosalie C,
Dai MuShui
Publication year - 2021
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.202050684
Subject(s) - deubiquitinating enzyme , sumo protein , ribosome biogenesis , biogenesis , small nucleolar rna , ribosome , biology , microbiology and biotechnology , chemistry , genetics , rna , long non coding rna , ubiquitin , gene
SUMOylation plays a crucial role in regulating diverse cellular processes including ribosome biogenesis. Proteomic analyses and experimental evidence showed that a number of nucleolar proteins involved in ribosome biogenesis are modified by SUMO. However, how these proteins are SUMOylated in cells is less understood. Here, we report that USP36, a nucleolar deubiquitinating enzyme (DUB), promotes nucleolar SUMOylation. Overexpression of USP36 enhances nucleolar SUMOylation, whereas its knockdown or genetic deletion reduces the levels of SUMOylation. USP36 interacts with SUMO2 and Ubc9 and directly mediates SUMOylation in cells and in vitro . We show that USP36 promotes the SUMOylation of the small nucleolar ribonucleoprotein (snoRNP) components Nop58 and Nhp2 in cells and in vitro and their binding to snoRNAs. It also promotes the SUMOylation of snoRNP components Nop56 and DKC1. Functionally, we show that knockdown of USP36 markedly impairs rRNA processing and translation. Thus, USP36 promotes snoRNP group SUMOylation and is critical for ribosome biogenesis and protein translation.