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The deubiquitinase USP36 promotes snoRNP group SUMOylation and is essential for ribosome biogenesis.
Ryu, Hyunju; Sun, Xiao-Xin; Chen, Yingxiao; Li, Yanping; Wang, Xiaoyan; Dai, Roselyn S; Zhu, Hong-Ming; Klimek, John; David, Larry; Fedorov, Lev M; Azuma, Yoshiaki; Sears, Rosalie C; Dai, Mu-Shui.
Afiliação
  • Ryu H; Department of Molecular & Medical Genetics, Oregon Health & Science University, Portland, OR, USA.
  • Sun XX; Department of Molecular & Medical Genetics, Oregon Health & Science University, Portland, OR, USA.
  • Chen Y; Department of Molecular & Medical Genetics, Oregon Health & Science University, Portland, OR, USA.
  • Li Y; Department of Molecular & Medical Genetics, Oregon Health & Science University, Portland, OR, USA.
  • Wang X; Department of Molecular & Medical Genetics, Oregon Health & Science University, Portland, OR, USA.
  • Dai RS; Department of Molecular & Medical Genetics, Oregon Health & Science University, Portland, OR, USA.
  • Zhu HM; Department of Molecular & Medical Genetics, Oregon Health & Science University, Portland, OR, USA.
  • Klimek J; Department of Chemical Physiology & Biochemistry, School of Medicine, Oregon Health & Science University, Portland, OR, USA.
  • David L; OHSU Proteomics Shared Resource, Oregon Health & Science University, Portland, OR, USA.
  • Fedorov LM; Department of Chemical Physiology & Biochemistry, School of Medicine, Oregon Health & Science University, Portland, OR, USA.
  • Azuma Y; OHSU Proteomics Shared Resource, Oregon Health & Science University, Portland, OR, USA.
  • Sears RC; OHSU Transgenic Mouse Models Shared Resource, Oregon Health & Science University, Portland, OR, USA.
  • Dai MS; Department of Molecular Biosciences, University of Kansas, Lawrence, KS, USA.
EMBO Rep ; 22(6): e50684, 2021 06 04.
Article em En | MEDLINE | ID: mdl-33852194
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.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Ribonucleoproteínas Nucleolares Pequenas / Sumoilação Limite: Humans Idioma: En Ano de publicação: 2021 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Ribonucleoproteínas Nucleolares Pequenas / Sumoilação Limite: Humans Idioma: En Ano de publicação: 2021 Tipo de documento: Article