{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T11:10:56Z","timestamp":1790334656230,"version":"4.1.0"},"reference-count":119,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T00:00:00Z","timestamp":1790294400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Mol. Neurosci."],"abstract":"<jats:p>Neurons rely on precise protein folding, trafficking, and turnover to maintain synaptic function. Disruption of proteostasis promotes misfolded proteins that impair axonal transport, mitochondrial function, and signalling, contributing to neuronal loss. Although neurodegeneration has traditionally focused on stable amyloid deposits, many disease-associated proteins contain intrinsically disordered regions (IDRs) that can organize through liquid\u2013liquid phase separation (LLPS). LLPS concentrates proteins and nucleic acids into dynamic condensates that regulate cellular processes, but these adaptive interactions can also promote condensate aging and less reversible, aggregation-prone states. Here, we review how sequence-encoded properties of tau and \u03b1-synuclein (\u03b1-syn) link physiological condensation to pathological protein assembly, while emphasizing that LLPS and amyloid formation are related but not obligatorily linked.<\/jats:p>","DOI":"10.3389\/fnmol.2026.1965177","type":"journal-article","created":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T10:50:52Z","timestamp":1790333452000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":0,"title":["From dynamic condensates to pathological assemblies: the phase behavior of tau and \u03b1-synuclein"],"prefix":"10.3389","volume":"19","author":[{"given":"Suelen","family":"Camargo","sequence":"first","affiliation":[{"name":"Department of Clinical Neuroscience, University of Calgary","place":["Calgary, AB, Canada"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kevin","family":"Novelo","sequence":"additional","affiliation":[{"name":"Department of Clinical Neuroscience, University of Calgary","place":["Calgary, AB, Canada"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Scott D.","family":"Ryan","sequence":"additional","affiliation":[{"name":"Department of Clinical Neuroscience, University of Calgary","place":["Calgary, AB, Canada"]},{"name":"Department of Physiology and Pharmacology, University of Calgary","place":["Calgary, AB, Canada"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2026,9,25]]},"reference":[{"key":"ref1","doi-asserted-by":"publisher","first-page":"251","DOI":"10.1038\/s42003-024-05920-4","article-title":"Phosphorylation regulates tau\u2019s phase separation behavior and interactions with chromatin","volume":"7","author":"Abasi","year":"2024","journal-title":"Commun. 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