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Nuclear LSm8 affects number of cytoplasmic processing bodies via controlling cellular distribution of Like-Sm proteins
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SYSNO ASEP 0381677 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Nuclear LSm8 affects number of cytoplasmic processing bodies via controlling cellular distribution of Like-Sm proteins Author(s) Novotný, Ivan (UMG-J)
Podolská, Kateřina (UMG-J)
Blažíková, Michaela (UEM-P)
Valášek, Leoš Shivaya (MBU-M) RID, ORCID
Svoboda, Petr (UMG-J) RID, ORCID
Staněk, David (UMG-J) RIDSource Title Molecular Biology of the Cell - ISSN 1059-1524
Roč. 23, č. 19 (2012), s. 3776-3785Number of pages 10 s. Language eng - English Country US - United States Keywords P-bodies ; LSm proteins ; mRNA degradation Subject RIV EB - Genetics ; Molecular Biology R&D Projects KAN200520801 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) GA204/07/0133 GA ČR - Czech Science Foundation (CSF) GAP305/10/2215 GA ČR - Czech Science Foundation (CSF) GAP302/11/1910 GA ČR - Czech Science Foundation (CSF) GBP305/12/G034 GA ČR - Czech Science Foundation (CSF) Institutional support UMG-J - RVO:68378050 ; UEM-P - RVO:68378041 ; MBU-M - RVO:61388971 CEZ AV0Z50390703 - UEM-P (2007-2013) AV0Z50520514 - UMG-J (2005-2011) AV0Z50200510 - MBU-M (2005-2011) UT WOS 000312223300002 DOI https://doi.org/10.1091/mbc.E12-02-0085 Annotation Processing bodies (P-bodies) are dynamic cytoplasmic structures involved in mRNA degradation, but the mechanism that governs their formation is poorly understood. In this paper, we address a role of Like-Sm (LSm) proteins in formation of P-bodies and provide evidence that depletion of nuclear LSm8 increases the number of P-bodies, while LSm8 overexpression leads to P-body loss. We show that LSm8 knockdown causes relocalization of LSm4 and LSm6 proteins to the cytoplasm and suggest that LSm8 controls nuclear accumulation of all LSm2-7 proteins. We propose a model in which redistribution of LSm2-7 to the cytoplasm creates new binding sites for other P-body components and nucleates new, microscopically visible structures. The model is supported by prolonged residence of two P-body proteins, DDX6 and Ago2, in P-bodies after LSm8 depletion, which indicates stronger interactions between these proteins and P-bodies. Finally, an increased number of P-bodies has negligible effects on microRNA-mediated translation repression and nonsense mediated decay, further supporting the view that the function of proteins localized in P-bodies is independent of visible P-bodies. Workplace Institute of Molecular Genetics Contact Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Year of Publishing 2013
Number of the records: 1