Phospho-dependent phase separation of FMRP and CAPRIN1 recapitulates regulation of translation and deadenylation

• DOI: 10.1126/science.aax4240
• Publication Date: 2019-09-03T21:36:26Z
• Authors: Tae Hun Kim; Brian Tsang; Robert M. Vernon; Nahum Sonenberg; Lewis E. Kay; Julie D. Forman-Kay
• Keywords: Separation (statistics)

Membraneless organelles involved in RNA processing are biomolecular condensates assembled by phase separation. Despite the important role of intrinsically disordered protein regions (IDRs), specific interactions underlying IDR separation and its functional consequences remain elusive. To address these questions, we used minimal formed from C-terminal two interacting translational regulators, FMRP CAPRIN1. Nuclear magnetic resonance spectroscopy FMRP-CAPRIN1 revealed involving arginine-rich aromatic-rich regions. We found that different serine/threonine CAPRIN1 tyrosine phosphorylation patterns control propensity with RNA, including subcompartmentalization, tune deadenylation translation rates vitro. The resulting evidence for residue-specific co-phase separation, phosphorylation-modulated condensate architecture, enzymatic activity within has implications how integration signaling pathways controls translation.