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Selective Ion Binding and Uptake Shape the Microenvironment of Biomolecular Condensates
1. Introduction Click to copy section linkSection link copied! Biomolecular condensates are phase-separated compartments that regulate a variety of cellular processes, including ribosome biogenesis, stress response, and protein aggregation. (1,2) They are formed through multivalent interactions between proteins and, in some cases, RNA, resulting in droplets that are enriched in biomolecules and have distinct local physicochemical environments.
A cyclin-dependent kinase-mediated phosphorylation switch of disordered protein condensation - Nature Communications
Abstract Cell cycle transitions result from global changes in protein phosphorylation states triggered by cyclin-dependent kinases (CDKs). To understand how this complexity produces an ordered and rapid cellular reorganisation, we generated a high-resolution map of changing phosphosites throughout unperturbed early cell cycles in single Xenopus embryos, derived the emergent principles through systems biology analysis, and tested them by biophysical modelling and biochemical experiments.
The structure of pathogenic huntingtin exon 1 defines the bases of its aggregation propensity - Nature Structural & Molecular Biology
Abstract Huntington’s disease is a neurodegenerative disorder caused by a CAG expansion in the first exon of the HTT gene, resulting in an extended polyglutamine (poly-Q) tract in huntingtin (httex1). The structural changes occurring to the poly-Q when increasing its length remain poorly understood due to its intrinsic flexibility and the strong compositional bias.
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