A CAF40-binding motif facilitates recruitment of the CCR4-NOT complex to mRNAs targeted by Drosophila Roquin

Annamaria Sgromo, Tobias Raisch, Praveen Bawankar, Dipankar Bhandari, Ying Chen, Duygu Kuzuoğlu-Öztürk, Oliver Weichenrieder and Elisa Izaurralde ()
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Annamaria Sgromo: Max Planck Institute for Developmental Biology
Tobias Raisch: Max Planck Institute for Developmental Biology
Praveen Bawankar: Max Planck Institute for Developmental Biology
Dipankar Bhandari: Max Planck Institute for Developmental Biology
Ying Chen: Max Planck Institute for Developmental Biology
Duygu Kuzuoğlu-Öztürk: Max Planck Institute for Developmental Biology
Oliver Weichenrieder: Max Planck Institute for Developmental Biology
Elisa Izaurralde: Max Planck Institute for Developmental Biology

Nature Communications, 2017, vol. 8, issue 1, 1-16

Abstract: Abstract Human (Hs) Roquin1 and Roquin2 are RNA-binding proteins that promote mRNA target degradation through the recruitment of the CCR4-NOT deadenylase complex and are implicated in the prevention of autoimmunity. Roquin1 recruits CCR4-NOT via a C-terminal region that is not conserved in Roquin2 or in invertebrate Roquin. Here we show that Roquin2 and Drosophila melanogaster (Dm) Roquin also interact with the CCR4-NOT complex through their C-terminal regions. The C-terminal region of Dm Roquin contains multiple motifs that mediate CCR4-NOT binding. One motif binds to the CAF40 subunit of the CCR4-NOT complex. The crystal structure of the Dm Roquin CAF40-binding motif (CBM) bound to CAF40 reveals that the CBM adopts an α-helical conformation upon binding to a conserved surface of CAF40. Thus, despite the lack of sequence conservation, the C-terminal regions of Roquin proteins act as an effector domain that represses the expression of mRNA targets via recruitment of the CCR4-NOT complex.

Date: 2017
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DOI: 10.1038/ncomms14307

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