Insights into the assembly and architecture of a Staufen-mediated mRNA decay (SMD)-competent mRNP

Manjeera Gowravaram, Juliane Schwarz, Sana K. Khilji, Henning Urlaub and Sutapa Chakrabarti ()
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Manjeera Gowravaram: Freie Universität Berlin
Juliane Schwarz: Max Planck Institute for Biophysical Chemistry
Sana K. Khilji: Freie Universität Berlin
Henning Urlaub: Max Planck Institute for Biophysical Chemistry
Sutapa Chakrabarti: Freie Universität Berlin

Nature Communications, 2019, vol. 10, issue 1, 1-14

Abstract: Abstract The mammalian Staufen proteins (Stau1 and Stau2) mediate degradation of mRNA containing complex secondary structures in their 3’-untranslated region (UTR) through a pathway known as Staufen-mediated mRNA decay (SMD). This pathway also involves the RNA helicase UPF1, which is best known for its role in the nonsense-mediated mRNA decay (NMD) pathway. Here we present a biochemical reconstitution of the recruitment and activation of UPF1 in context of the SMD pathway. We demonstrate the involvement of UPF2, a core NMD factor and a known activator of UPF1, in SMD. UPF2 acts as an adaptor between Stau1 and UPF1, stimulates the catalytic activity of UPF1 and plays a central role in the formation of an SMD-competent mRNP. Our study elucidates the molecular mechanisms of SMD and points towards extensive cross-talk between UPF1-mediated mRNA decay pathways in cells.

Date: 2019
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DOI: 10.1038/s41467-019-13080-x

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