Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
A new study reveals that extracellular signals can activate a signal-transduction cascade that simultaneously alters alternative splicing and translation of the same target. These concerted efforts probably serve to increase the speed and strength of the cellular response to changes in the extracellular environment.
Eukaryotic messenger RNAs are degraded through a pathway that starts with the removal of the poly(A) tail. A recent study shows that cytoplasmic mRNA deadenylation in mammals occurs by the consecutive action of two distinct deadenylases and that degradation of nonsense mRNA involves the same biphasic deadenylation pathway.
A new study sheds light on the mechanism regulating the translation of localized mRNAs at their destination. Phosphorylation of an RNA-binding protein by Src promotes complex disassembly and allows translation of the localized transcript.
The induction and repair of chromosome breaks is associated with myriad changes in chromatin. A recent study shows that chromatin remodeling that results in histone eviction at the break site requires the Mre11 complex and INO80 and that these events are important for efficient loading of the Rad51 recombinase.