Unknown

Dataset Information

0

A paradigm for regulation at the effector interface with RNA-binding proteins.


ABSTRACT: RNA-binding proteins (RBPs) are key regulators of gene expression, but how 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 deeply 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 the recruiting RBP. Systems analyses reveal that multivalent RBP-effector contacts can repurpose the principal activity of an effector for a different function, as we demonstrate for 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, with implications for the evolution and function of RBP-operated regulatory networks.

SUBMITTER: Shah K 

PROVIDER: S-EPMC10542489 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

A paradigm for regulation at the effector interface with RNA-binding proteins.

Shah Kriti K   He Shiyang S   Turner David J DJ   Corbo Joshua J   Rebbani Khadija K   Bateman Joseph M JM   Cheloufi Sihem S   Igreja Cátia C   Valkov Eugene E   Murn Jernej J  

bioRxiv : the preprint server for biology 20231024


RNA-binding proteins (RBPs) are key regulators of gene expression, but how 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 deeply 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. Unexpe  ...[more]

Similar Datasets

| S-EPMC11009413 | biostudies-literature
2024-04-11 | PXD050601 | Pride
| S-EPMC10242446 | biostudies-literature
2024-03-16 | GSE240571 | GEO
2024-03-17 | GSE240565 | GEO
2024-03-17 | GSE240562 | GEO
2024-03-17 | GSE240563 | GEO
2024-03-17 | GSE240568 | GEO
| PRJNA1004243 | ENA
| S-EPMC7710910 | biostudies-literature