Multifunctional deadenylase complexes diversify mRNA control
Top Cited Papers
- 1 April 2008
- journal article
- research article
- Published by Springer Nature in Nature Reviews Molecular Cell Biology
- Vol. 9 (4) , 337-344
- https://doi.org/10.1038/nrm2370
Abstract
Deadenylases shorten mRNA poly(A) tails and thereby regulate mRNA translation and decay. Recent studies have shown that these factors form different complexes. The recruitment of multifunctional deadenylase complexes to target mRNAs provides a unique node to control mRNA translation and decay. Dynamic changes of the lengths of mRNA poly(A) tails are catalysed by diverse deadenylase enzymes. Modulating the length of the poly(A) tail of an mRNA is a widespread means of controlling protein production and mRNA stability. Recent insights illuminate the specialized activities, biological functions and regulation of deadenylases. We propose that the recruitment of multifunctional deadenylase complexes provides unique opportunities to control mRNAs and that the heterogeneity of the deadenylase complexes is exploited to control translation and mRNA stability.Keywords
This publication has 76 references indexed in Scilit:
- Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylasesGenes & Development, 2007
- RNA Quality Control in EukaryotesCell, 2007
- Widespread use of poly(A) tail length control to accentuate expression of the yeast transcriptomeRNA, 2007
- A Network of Multiple Regulatory Layers Shapes Gene Expression in Fission YeastMolecular Cell, 2007
- The highways and byways of mRNA decayNature Reviews Molecular Cell Biology, 2007
- Conservation of the deadenylase activity of proteins of the Caf1 family in humanRNA, 2005
- RNA-Binding Proteins in Early DevelopmentCritical Reviews in Biochemistry and Molecular Biology, 2005
- The roles of cytoplasmic poly(A)-binding proteins in regulating gene expression: A developmental perspectiveBriefings in Functional Genomics and Proteomics, 2004
- X‐ray structure and activity of the yeast Pop2 protein: a nuclease subunit of the mRNA deadenylase complexEMBO Reports, 2003
- Ccr4p is the catalytic subunit of a Ccr4p/Pop2p/Notp mRNA deadenylase complex inSaccharomyces cerevisiaeThe EMBO Journal, 2002