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

Sgromo, A; Raisch, T; Bawankar, P; Bhandari, D; Chen, Y; Kuzuoğlu-Öztürk, D; Weichenrieder, O; Izaurralde, E

doi:10.1038/ncomms14307

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

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

/persons/resource/persons229229

Raisch, T
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons273085

Bawankar, P
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons273087

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

/persons/resource/persons271770

Chen, Y
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons273089

Kuzuoğlu-Öztürk, D
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons271778

Weichenrieder, O
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;
Retrotransposition and Regulatory RNAs Group, Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons271767

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

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Citation

Sgromo, A., Raisch, T., Bawankar, P., Bhandari, D., Chen, Y., Kuzuoğlu-Öztürk, D., et al. (2017). A CAF40-binding motif facilitates recruitment of the CCR4-NOT complex to mRNAs targeted by Drosophila Roquin. Nature Communications, 8: 14307. doi:10.1038/ncomms14307.

Cite as: https://hdl.handle.net/21.11116/0000-0002-136E-E

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 a-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.