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First published online 10 February 2009
doi: 10.1242/jcs.044461

Journal of Cell Science 122, 678-686 (2009)
Published by The Company of Biologists 2009
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Research Article

Nucleolar structure and function are regulated by the deubiquitylating enzyme USP36

Akinori Endo1, Masaki Matsumoto2, Toshifumi Inada3, Akitsugu Yamamoto4, Keiichi I. Nakayama2, Naomi Kitamura1 and Masayuki Komada1,*

1 Department of Biological Sciences, Tokyo Institute of Technology, Yokohama 226-8501, Japan
2 Department of Molecular and Cellular Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan
3 Department of Molecular Biology, Nagoya University, Nagoya 464-8602, Japan
4 Department of Bio-science, Nagahama Institute of Bio-science and Technology, Nagahama 526-0829, Japan

* Author for correspondence (e-mail: makomada{at}bio.titech.ac.jp)

Accepted 18 November 2008

The nucleolus is a subnuclear compartment and the site of ribosome biogenesis. Previous studies have implicated protein ubiquitylation in nucleolar activity. Here we show that USP36, a deubiquitylating enzyme of unknown function, regulates nucleolar activity in mammalian cells. USP36 localized to nucleoli via the C-terminal region, which contains basic amino acid stretches. Dominant-negative inhibition of USP36 caused the accumulation of ubiquitin-protein conjugates in nucleoli, suggesting that nucleoli are the site of USP36 action. USP36 deubiquitylated the nucleolar proteins nucleophosmin/B23 and fibrillarin, and stabilized them by counteracting ubiquitylation-mediated proteasomal degradation. RNAi-mediated depletion of cellular USP36 resulted in reduced levels of rRNA transcription and processing, a less-developed nucleolar morphology and a slight reduction in the cytoplasmic ribosome level, which eventually led to a reduced rate of cell proliferation. We conclude that by deubiquitylating various nucleolar substrate proteins including nucleophosmin/B23 and fibrillarin, USP36 plays a crucial role in regulating the structure and function of nucleoli.

Key words: Deubiquitylating enzyme, Nucleolus, Protein degradation, Ribosome biogenesis, rRNA


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Related articles in JCS:

Undoing ubiquitylation in nucleoli

JCS 2009 122: 501. [Full Text]  



This article has been cited by other articles:


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 J. Biol. Chem.Home page
A. Endo, N. Kitamura, and M. Komada
Nucleophosmin/B23 Regulates Ubiquitin Dynamics in Nucleoli by Recruiting Deubiquitylating Enzyme USP36
J. Biol. Chem., October 9, 2009; 284(41): 27918 - 27923.
[Abstract] [Full Text] [PDF]


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