5LSW

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

Summary for 5LSW

• Entry DOI: 10.2210/pdb5lsw/pdb
• Descriptor: Cell differentiation protein RCD1 homolog, LD12033p, SULFATE ION, ... (5 entities in total)
• Functional Keywords: gene regulation, deadenylation, ccr4-not, translational repression, translation
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus : Q92600
• Total number of polymer chains: 4
• Total formula weight: 67328.10

Authors

Sgromo, A.,Raisch, T.,Bawankar, P.,Bhandari, D.,Chen, Y.,Kuzuoglu-Ozturk, D.,Weichenrieder, O.,Izaurralde, E. (deposition date: 2016-09-05, release date: 2017-02-15, Last modification date: 2024-01-17)

Primary citation

Sgromo, A.,Raisch, T.,Bawankar, P.,Bhandari, D.,Chen, Y.,Kuzuoglu-Ozturk, D.,Weichenrieder, O.,Izaurralde, E.
A CAF40-binding motif facilitates recruitment of the CCR4-NOT complex to mRNAs targeted by Drosophila Roquin.
Nat Commun, 8:14307-14307, 2017

PubMed 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.

PubMed: 28165457
DOI: 10.1038/ncomms14307

Experimental method

X-RAY DIFFRACTION (2.15 Å)