Binding of NUFIP2 to Roquin promotes recognition and regulation of ICOS mRNA
Nina Rehage,
Elena Davydova,
Christine Conrad,
Gesine Behrens,
Andreas Maiser,
Jenny E. Stehklein,
Sven Brenner,
Juliane Klein,
Aicha Jeridi,
Anne Hoffmann,
Eunhae Lee,
Umberto Dianzani,
Rob Willemsen,
Regina Feederle,
Kristin Reiche,
Jörg Hackermüller,
Heinrich Leonhardt,
Sonia Sharma (),
Dierk Niessing () and
Vigo Heissmeyer ()
Additional contact information
Nina Rehage: Ludwig-Maximilians-Universität München
Elena Davydova: Helmholtz Zentrum München
Christine Conrad: Ludwig-Maximilians-Universität München
Gesine Behrens: Ludwig-Maximilians-Universität München
Andreas Maiser: Ludwig-Maximilians-Universität München
Jenny E. Stehklein: Helmholtz Zentrum München
Sven Brenner: Helmholtz Zentrum München
Juliane Klein: Ludwig-Maximilians-Universität München
Aicha Jeridi: Helmholtz Zentrum München
Anne Hoffmann: Helmholtz Centre for Environmental Research – UFZ
Eunhae Lee: La Jolla Institute for Allergy and Immunology
Umberto Dianzani: Universita’ del Piemonte Orientale
Rob Willemsen: Erasmus MC
Regina Feederle: Helmholtz Zentrum München
Kristin Reiche: Fraunhofer Institute for Cell Therapy and Immunology- IZI
Jörg Hackermüller: Helmholtz Centre for Environmental Research – UFZ
Heinrich Leonhardt: Ludwig-Maximilians-Universität München
Sonia Sharma: La Jolla Institute for Allergy and Immunology
Dierk Niessing: Helmholtz Zentrum München
Vigo Heissmeyer: Ludwig-Maximilians-Universität München
Nature Communications, 2018, vol. 9, issue 1, 1-15
Abstract:
Abstract 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.
Date: 2018
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-017-02582-1
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DOI: 10.1038/s41467-017-02582-1
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