| Added by | mollevi |
|---|---|
| Last modified by | alainmange |
| Group name | PlateformePP2I |
| Item Type | Journal Article |
| Title | PIP30/FAM192A is a novel regulator of the nuclear proteasome activator PA28? |
| Creator | Jonik-Nowak et al. |
| Author | Beata Jonik-Nowak |
| Author | Thomas Menneteau |
| Author | Didier Fesquet |
| Author | Véronique Baldin |
| Author | Catherine Bonne-Andrea |
| Author | Bertrand Fabre |
| Author | Prisca Boisguerin |
| Author | Sylvain de Rossi |
| Author | Corinne Henriquet |
| Author | Martine Pugnière |
| Author | Manuelle Ducoux-Petit |
| Author | Odile Burlet-Schiltz |
| Author | Angus I. Lamond |
| Author | Philippe Fort |
| Author | Séverine Boulon |
| Author | Marie-Pierre Bousquet |
| Author | Olivier Coux |
| Abstract | PA28? is a nuclear activator of the 20S proteasome involved in the regulation of several essential cellular processes, such as cell proliferation, apoptosis, nuclear dynamics, and cellular stress response. Unlike the 19S regulator of the proteasome, which specifically recognizes ubiquitylated proteins, PA28? promotes the degradation of several substrates by the proteasome in an ATP- and ubiquitin-independent manner. However, its exact mechanisms of action are unclear and likely involve additional partners that remain to be identified. Here we report the identification of a cofactor of PA28?, PIP30/FAM192A. PIP30 binds directly and specifically via its C-terminal end and in an interaction stabilized by casein kinase 2 phosphorylation to both free and 20S proteasome-associated PA28?. Its recruitment to proteasome-containing complexes depends on PA28? and its expression increases the association of PA28? with the 20S proteasome in cells. Further dissection of its possible roles shows that PIP30 alters PA28?-dependent activation of peptide degradation by the 20S proteasome in vitro and negatively controls in cells the presence of PA28? in Cajal bodies by inhibition of its association with the key Cajal body component coilin. Taken together, our data show that PIP30 deeply affects PA28? interactions with cellular proteins, including the 20S proteasome, demonstrating that it is an important regulator of PA28? in cells and thus a new player in the control of the multiple functions of the proteasome within the nucleus. |
| Publication | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 115 |
| Issue | 28 |
| Pages | E6477-E6486 |
| Date | 07 10, 2018 |
| Journal Abbr | Proc. Natl. Acad. Sci. U.S.A. |
| Language | eng |
| DOI | 10.1073/pnas.1722299115 |
| ISSN | 1091-6490 |
| Library Catalog | PubMed |
| Extra | PMID: 29934401 PMCID: PMC6048556 |
| Tags | author, Autoantigens, Cajal bodies, Cell Nucleus, FAM192A, HeLa Cells, Humans, Nuclear Proteins, nuclear proteolysis, original, PA28?, pp2i, Proteasome Endopeptidase Complex, Protein Binding, Protein Domains, Proteins |
| Date Added | 2019/06/04 - 17:21:00 |
| Date Modified | 2020/01/14 - 10:25:19 |
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