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First published online 8 July 2008
doi: 10.1242/jcs.024976

Journal of Cell Science 121, 2463-2472 (2008)
Published by The Company of Biologists 2008
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Research Article

A role for Q/N-rich aggregation-prone regions in P-body localization

Martin A. M. Reijns*, Ross D. Alexander, Michael P. Spiller{ddagger} and Jean D. Beggs§

Wellcome Trust Centre for Cell Biology, University of Edinburgh, King's Buildings, Mayfield Road, Edinburgh EH9 3JR, UK

§ Author for correspondence (email: jbeggs{at}ed.ac.uk)

Accepted 14 May 2008

P-bodies are cytoplasmic foci that are sites of mRNA degradation and translational repression. It is not known what causes the accumulation of RNA-degradation factors in P-bodies, although RNA is required. The yeast Lsm1-7p complex (comprising Lsm1p to Lsm7p) is recruited to P-bodies under certain stress conditions. It is required for efficient decapping and degradation of mRNAs, but not for the assembly of P-bodies. Here we show that the Lsm4p subunit and its asparagine-rich C-terminus are prone to aggregation, and that this tendency to aggregate promotes efficient accumulation of Lsm1-7p in P-bodies. The presence of glutamine- and/or asparagine-rich (Q/N-rich) regions in other P-body components suggests a more general role for aggregation-prone residues in P-body localization and assembly. This is supported by reduced P-body accumulation of Ccr4p, Pop2p and Dhh1p after deletion of these domains, and by the observed aggregation of the Q/N-rich region from Ccr4p.

Key words: P-body localization, Protein aggregation, Q/N-rich domains, Stress


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This article has been cited by other articles:


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N. Minshall, M. Kress, D. Weil, and N. Standart
Role of p54 RNA Helicase Activity and Its C-terminal Domain in Translational Repression, P-body Localization and Assembly
Mol. Biol. Cell, May 1, 2009; 20(9): 2464 - 2472.
[Abstract] [Full Text] [PDF]


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