@article{bb8f2fff54f84ac98271e4091a803466,
title = "The deubiquitinase USP36 promotes snoRNP group SUMOylation and is essential for ribosome biogenesis",
abstract = "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.",
keywords = "SUMOylation, USP36, deubiquitinating enzyme, ribosome biogenesis, snoRNP",
author = "Hyunju Ryu and Sun, {Xiao Xin} and Yingxiao Chen and Yanping Li and Xiaoyan Wang and Dai, {Roselyn S.} and Zhu, {Hong Ming} and John Klimek and Larry David and Fedorov, {Lev M.} and Yoshiaki Azuma and Sears, {Rosalie C.} and Dai, {Mu Shui}",
note = "Funding Information: We thank Dr. Lionel Tafforeau (University of Mons, Belgium) and Dr. Jingyan Wu (Stanford University, San Francisco, USA) for sharing their Northern blot protocol and expertise and Dr. Masayuki Komada (Tokyo Institute of Technology, Japan) for providing reagents. We gratefully acknowledge OHSU Transgenic Core for generating the USP36 knockout mice and Mr. John Klimek for assistance with the mass spectrometry analysis. We thank the members from the Dai and Sears laboratories for active discussion. This work was supported by grants from NIH (R01 CA160474 and R01 GM130604 to M.-S.D. and R01 CA186241 to M.-S.D. and R.C.S.). Proteomic analysis was partially supported by NIH grants P30 EY010572, P30 CA069533, and S10 RR025571. Funding Information: We thank Dr. Lionel Tafforeau (University of Mons, Belgium) and Dr. Jingyan Wu (Stanford University, San Francisco, USA) for sharing their Northern blot protocol and expertise and Dr. Masayuki Komada (Tokyo Institute of Technology, Japan) for providing reagents. We gratefully acknowledge OHSU Transgenic Core for generating the USP36 knockout mice and Mr. John Klimek for assistance with the mass spectrometry analysis. We thank the members from the Dai and Sears laboratories for active discussion. This work was supported by grants from NIH (R01 CA160474 and R01 GM130604 to M.‐S.D. and R01 CA186241 to M.‐S.D. and R.C.S.). Proteomic analysis was partially supported by NIH grants P30 EY010572, P30 CA069533, and S10 RR025571. Publisher Copyright: {\textcopyright} 2021 The Authors",
year = "2021",
month = jun,
day = "4",
doi = "10.15252/embr.202050684",
language = "English (US)",
volume = "22",
journal = "EMBO Reports",
issn = "1469-221X",
publisher = "Nature Publishing Group",
number = "6",
}