Two new publications are out

Somatic increase of CCT8 mimics proteostasis of human pluripotent stem cells and extends C. elegans lifespan.

Noormohammadi A, Khodakarami A, Gutierrez-Garcia R, Lee HJ, Koyuncu S, König T, Schindler C, Saez I, Fatima A, Dieterich C, Vilchez D.

Nat Commun. 2016 Nov 28;7:13649. doi: 10.1038/ncomms13649.

PMID: 27892468

Reducing RBM20 activity improves diastolic dysfunction and cardiac atrophy.

Hinze F, Dieterich C, Radke MH, Granzier H, Gotthardt M.

J Mol Med (Berl). 2016 Nov 26. [Epub ahead of print]

PMID: 27889803

Nature Communications manuscript accepted

Aside

Title: Mondo complexes regulate TFEB via TOR inhibition to promote longevity in response to gonadal signals

Authors: Shuhei Nakamura, Özlem Karalay, Philipp S. Jäger, MakotoHorikawa, Corinna Klein, Kayo Nakamura, Christian Latza, Sven E. Templer, Christoph Dieterich & Adam Antebi

Joint work with our dear colleagues from the MPI-AGE was accepted for publication
in Nature Communications.

New manuscript is out – MOV10 Is a 5′ to 3′ RNA Helicase Contributing to UPF1 mRNA Target Degradation by Translocation along 3′ UTRs.

Mol Cell. 2014 Apr 8. pii: S1097-2765(14)00222-6. doi: 10.1016/j.molcel.2014.03.017. [Epub ahead of print]

MOV10 Is a 5′ to 3′ RNA Helicase Contributing to UPF1 mRNA Target Degradation by Translocation along 3′ UTRs.

Abstract

RNA helicases are important regulators of gene expression that act by remodeling RNA secondary structures and RNA-protein interactions. Here, we demonstrate that MOV10 has an ATP-dependent 5′ to 3′ in vitro RNA unwinding activity and determine the RNA-binding sites of MOV10 and its helicase mutants using PAR-CLIP. We find that MOV10 predominantly binds to 3′ UTRs upstream of regions predicted to form local secondary structures and provide evidence that MOV10 helicase mutants are impaired in their ability to translocate 5′ to 3′ on their mRNA targets. MOV10 interacts with UPF1, the key component of the nonsense-mediated mRNA decay pathway. PAR-CLIP of UPF1 reveals that MOV10 and UPF1 bind to RNA in close proximity. Knockdown of MOV10 resulted in increased mRNA half-lives of MOV10-bound as well as UPF1-regulated transcripts, suggesting that MOV10 functions in UPF1-mediated mRNA degradation as an RNA clearance factor to resolve structures and displace proteins from 3′ UTRs.