Article

Phase separation behavior of TDP-43 governs its protein interactome and regulation of alternative splicing

2026-04-07

Abstract excerpt

<h4>Summary</h4> TDP-43 is a nuclear RNA-binding protein that regulates RNA metabolism, including alternative splicing. Its aggregation is a major pathological hallmark of several neurodegenerative diseases. TDP-43 undergoes phase separation (PS) and this condensation behavior may be linked to aggregate formation. Whether and how PS governs TDP-43’s RNA regulatory functions remains poorly understood. Here we util...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 45d77166-a5bf-56c5-b812-3dea9d99a339
DOI: 10.64898/2026.04.06.716630

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Phase separation behavior of TDP-43 governs its protein interactome and regulation of alternative splicingDOI 10.64898/2026.04.06.716630Read

SUMO paralogues differentially affect phase separation and aggregation of intrinsically disordered proteinsSemantic proximity Read

Cellular modifiers of TDP-43 phase transition and cytoplasmic aggregationSemantic proximity Read

Proteomics Elucidating Physiological and Pathological Functions of TDP-43Semantic proximity Read

TAR DNA-binding protein 43 (TDP-43) liquid-liquid phase separation is mediated by just a few aromatic residues.Semantic proximity Read

TDP-43 condensation properties specify its RNA-binding and regulatory repertoire.Semantic proximity Read

Disease-linked TDP-43 hyperphosphorylation suppresses TDP-43 condensation and aggregationSemantic proximity Read

Structural Insights Into TDP-43 and Effects of Post-translational ModificationsSemantic proximity Read

RNA-binding properties orchestrate TDP-43 homeostasis through condensate formation in vivo.Semantic proximity Read

Small heat shock proteins HspB1 and HspB5 differentially alter the condensation and aggregation of the TDP-43 low complexity domainSemantic proximity Read

Phase Separation as a Missing Mechanism for Interpretation of Disease Mutations.Semantic proximity Read

Multi-Domain Interplay Controls Full-Length TDP-43 Phase Separation and Condensate DynamicsSemantic proximity Read

Phase Behavior of TDP-43 and hnRNPH1: From Soluble and Aggregated States to Liquid-Like DropletsSemantic proximity Read