The deubiquitinase USP36 promotes snoRNP group SUMOylation and is essential for ribosome biogenesis. (14th April 2021)
- Record Type:
- Journal Article
- Title:
- The deubiquitinase USP36 promotes snoRNP group SUMOylation and is essential for ribosome biogenesis. (14th April 2021)
- Main Title:
- The deubiquitinase USP36 promotes snoRNP group SUMOylation and is essential for ribosome biogenesis
- Authors:
- 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 - Abstract:
- 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. SYNOPSIS: The deubiquitinase USP36 also promotes protein SUMOylation and is essential for ribosome biogenesis and protein translation. USP36 promotes nucleolar protein SUMOylation. USP36 is the first identified DUB/SUMO promoting dual function protein. USP36 promotes snoRNA protein group SUMOylation. USP36 is critical for rRNA processing, translation and cell growth. Abstract : TheAbstract: 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. SYNOPSIS: The deubiquitinase USP36 also promotes protein SUMOylation and is essential for ribosome biogenesis and protein translation. USP36 promotes nucleolar protein SUMOylation. USP36 is the first identified DUB/SUMO promoting dual function protein. USP36 promotes snoRNA protein group SUMOylation. USP36 is critical for rRNA processing, translation and cell growth. Abstract : The deubiquitinase USP36 also promotes protein SUMOylation and is essential for ribosome biogenesis and protein translation. … (more)
- Is Part Of:
- EMBO reports. Volume 22:Number 6(2021)
- Journal:
- EMBO reports
- Issue:
- Volume 22:Number 6(2021)
- Issue Display:
- Volume 22, Issue 6 (2021)
- Year:
- 2021
- Volume:
- 22
- Issue:
- 6
- Issue Sort Value:
- 2021-0022-0006-0000
- Page Start:
- n/a
- Page End:
- n/a
- Publication Date:
- 2021-04-14
- Subjects:
- deubiquitinating enzyme -- ribosome biogenesis -- snoRNP -- SUMOylation -- USP36
Molecular biology -- Periodicals
Molecular Biology -- Periodicals
Molecular biology
Periodicals
572.8 - Journal URLs:
- http://www.embo-reports.oupjournals.org/ ↗
http://onlinelibrary.wiley.com/ ↗
http://firstsearch.oclc.org ↗
http://firstsearch.oclc.org/journal=1469-221x;screen=info;ECOIP ↗ - DOI:
- 10.15252/embr.202050684 ↗
- Languages:
- English
- ISSNs:
- 1469-221X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3733.086000
British Library DSC - BLDSS-3PM
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- 23028.xml