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Journal Article

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

MPS-Authors
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Schwarz,  J.
Research Group of Sleep and Waking, MPI for biophysical chemistry, Max Planck Society;

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Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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3177391.pdf
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Supplementary Material (public)

3177391_Suppl.htm
(Supplementary material), 202KB

Citation

Gowravaram, M., Schwarz, J., Khilji, S. K., Urlaub, H., & Chakrabarti, S. (2019). Insights into the assembly and architecture of a Staufen-mediated mRNA decay (SMD)-competent mRNP. Nature Communications, 10(1): 5054. doi:10.1038/s41467-019-13080-x.


Cite as: http://hdl.handle.net/21.11116/0000-0005-3A86-3
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.