biostudies-literatureRyu HNational Eye InstituteNEI NIH HHSNCRR NIH HHSNational Cancer InstituteNCI NIH HHSNational Institute of General Medical SciencesNIGMS NIH HHSe50684https://www.ebi.ac.uk/biostudies/studies/S-EPMC8183414biostudies-literatureUnknown22(6)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 EMBO reportsThe deubiquitinase USP36 promotes snoRNP group SUMOylation and is essential for ribosome biogenesis.PMC8183414CA069533R01 CA160474R01 GM130604GM130604P30 CA069533EY010572S10 RR025571P30 EY010572R01 CA186241Klimek JAzuma YDai RSRyu HFedorov LMDai MSSun XXLi YSears RCChen YWang XZhu HMDavid LfalseThe deubiquitinase USP36 promotes snoRNP group SUMOylation and is essential for ribosome biogenesis.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 2021-01-01T00:00:00Z2021 Jun2025-04-18T14:13:08.412Z2025-04-07T00:13:06.238ZS-EPMC81834143385219410.15252/embr.202050684