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Recruiting the PAN2-PAN3 deadenylase complex to mRNA targets

MPS-Authors
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Christie,  M
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Boland,  A       
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Peter,  D       
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Huntzinger,  E       
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Bhandari,  D       
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Loh,  B       
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Weichenrieder,  O       
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Izaurralde,  E       
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Christie, M., jonas stephanie, Boland, A., Peter, D., Huntzinger, E., Bhandari, D., et al. (2017). Recruiting the PAN2-PAN3 deadenylase complex to mRNA targets. In 31st Biennial Conference of the Society of Crystallographers in Australia and New Zealand (SCANZ — CRYSTAL 31) (pp. 25).


Cite as: https://hdl.handle.net/21.11116/0000-000F-3A82-D
Abstract
mRNA degradation is an essential component of the gene expression process. Cytoplasmic mRNA
decay is typically initiated by the removal of poly(A) tails, a process termed deadenylation, which
causes translational repression and, in most cases, triggers irreversible mRNA degradation. The PAN2-
PAN3 deadenylase complex functions in both bulk and microRNA-mediated mRNA decay and is
directly recruited to microRNA targets by GW182/ TNRC6 proteins. Taking a structural and functional
approach, we have identified unusual features that mediate the interaction of PAN3 with PAN2 and
TNRC6 proteins, as well as critical residues required for mRNA degradation in vivo. Collectively, our
data describes the structural basis for the recruitment of the PAN2-PAN3 complex to microRNA
targets by the TNRC6 proteins, and the essential role of PAN3 in coordinating deadenylation with
downstream steps of the mRNA decay pathway.