Publications - Published papers

Please find below publications of our group. Currently, we list 500 papers. Some of the publications are in collaboration with the group of Sonja Prohaska and are also listed in the publication list for her individual group. Access to published papers (access) is restricted to our local network and chosen collaborators. If you have problems accessing electronic information, please let us know:

©NOTICE: All papers are copyrighted by the authors; If you would like to use all or a portion of any paper, please contact the author.

Binding of NUFIP2 to Roquin promotes recognition and regulation of ICOS mRNA

Rehage, Nina and Davydova, Elena and Conrad, Christine and Behrens, Gesine and Maiser, Andreas and Stehklein, Jenny E. and Brenner, Sven and Klein, Juliane and Jeridi, Aicha and Hoffmann, Anne and Lee, Eunhae and Dianzani, Umberto and Willemsen, Rob and Feederle, Regina and Reiche, Kristin and Hackermüller, Jörg and Leonhardt, Heinrich and Sharma, Sonia and Niessing, Dierk and Heissmeyer, Vigo


PREPRINT 18-045:


Nature Communications 9: 299


The ubiquitously expressed RNA-binding proteins Roquin-1 and Roquin-2 are essential for appropriate immune cell function and postnatal survival of mice. Roquin proteins repress target mRNAs by recognizing secondary structures in their 3′-UTRs and by inducing mRNA decay. However, it is unknown if other cellular proteins contribute to target control. To identify cofactors of Roquin, we used RNA interference to screen ~1500 genes involved in RNA-binding or mRNA degradation, and identified NUFIP2 as a cofactor of Roquin-induced mRNA decay. NUFIP2 binds directly and with high affinity to Roquin, which stabilizes NUFIP2 in cells. Post-transcriptional repression of human ICOS by endogenous Roquin proteins requires two neighboring non-canonical stem-loops in the ICOS 3′-UTR. This unconventional cis-element as well as another tandem loop known to confer Roquin-mediated regulation of the Ox40 3′-UTR, are bound cooperatively by Roquin and NUFIP2. NUFIP2 therefore emerges as a cofactor that contributes to mRNA target recognition by Roquin.