Regulation by the RNA-binding protein Unkempt at its effector interface

Kriti Shah, Shiyang He, David J. Turner, Joshua Corbo, Khadija Rebbani, Daniel Dominguez, Joseph M. Bateman, Sihem Cheloufi, Cátia Igreja, Eugene Valkov () and Jernej Murn ()
Additional contact information
Kriti Shah: Boyce Hall
Shiyang He: Boyce Hall
David J. Turner: National Cancer Institute
Joshua Corbo: National Cancer Institute
Khadija Rebbani: National Cancer Institute
Daniel Dominguez: University of North Carolina at Chapel Hill
Joseph M. Bateman: King’s College London
Sihem Cheloufi: Boyce Hall
Cátia Igreja: Max-Planck-Ring 9
Eugene Valkov: National Cancer Institute
Jernej Murn: Boyce Hall

Nature Communications, 2024, vol. 15, issue 1, 1-18

Abstract: Abstract How RNA-binding proteins (RBPs) convey regulatory instructions to the core effectors of RNA processing is unclear. Here, we document the existence and functions of a multivalent RBP–effector interface. We show that the effector interface of a conserved RBP with an essential role in metazoan development, Unkempt, is mediated by a novel type of ‘dual-purpose’ peptide motifs that can contact two different surfaces of interacting proteins. Unexpectedly, we find that the multivalent contacts do not merely serve effector recruitment but are required for the accuracy of RNA recognition by Unkempt. Systems analyses reveal that multivalent RBP–effector contacts can repurpose the principal activity of an effector for a different function, as we demonstrate for the reuse of the central eukaryotic mRNA decay factor CCR4-NOT in translational control. Our study establishes the molecular assembly and functional principles of an RBP–effector interface.

Date: 2024
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DOI: 10.1038/s41467-024-47449-4

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