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First published online February 18, 2009

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Undoing ubiquitylation in nucleoli

Nucleoli are subnuclear compartments in which many important cellular processes occur, including the biogenesis of ribosomes and the regulation of cell-cycle and stress responses. Previous work has shown that several nucleolar proteins can be ubiquitylated, but it has been unclear whether ubiquitin is important for the function of nucleoli. On page 678, Masayuki Komada and colleagues show that the deubiquitylation of two key nucleolar proteins that are involved in ribosome biogenesis – nucleophosmin (NPM) and fibrillarin (FBRL) – by ubiquitin-specific protease 36 (USP36) is essential for the normal organisation and function of nucleoli. USP36-mediated cleavage of ubiquitin moieties from NPM and FBRL stabilises these proteins and prevents their proteasomal degradation. If the expression or function of USP36 is inhibited, the levels of NPM and FBRL in nucleoli are decreased, ribosome biogenesis occurs at a suboptimal rate and cell proliferation is impaired. This work reveals an important role for ubiquitin in the function of nucleoli and defines USP36 as the first deubiquitylating enzyme with nucleolar localisation.

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Nucleolar structure and function are regulated by the deubiquitylating enzyme USP36

Akinori Endo, Masaki Matsumoto, Toshifumi Inada, Akitsugu Yamamoto, Keiichi I. Nakayama, Naomi Kitamura, and Masayuki Komada
JCS 2009 122: 678-686. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?