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Pathological TDP\u201043 aggregates have become a defining hallmark of neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and a large subset of frontotemporal lobar degeneration (FTLD). In the last decade, increasing evidence has challenged the initial thought of TDP\u201043 condensates as a purely pathological event, highlighting instead the physiological relevance of reversible self\u2010association, polymerization and liquid\u2010liquid phase separation (LLPS) in regulating TDP\u201043 functions. In this review, we provide an integrated overview of the structural determinants governing TDP\u201043 two\u2010faced polymerization, with a particular focus on the prion\u2010like domain and its parallelism with prion proteins. Indeed, while physiological assemblies support normal RNA processing, the dysregulation of LLPS by either disease\u2010associated mutations, altered RNA\u2010binding, aberrant post\u2010translational modifications, or proteolytic cleavage can promote the transition toward irreversible, pathogenic aggregates. Finally, we summarize strategies aimed at eliminating TDP\u201043 aggregates or modulating its phase\u2010separation behavior. Altogether, this review frames TDP\u201043 polymerization in both healthy and pathological conditions, offering a prion\u2010like centered view of TDP\u201043 proteinopathies.<\/jats:p>","DOI":"10.1002\/advs.76119","type":"journal-article","created":{"date-parts":[[2026,6,15]],"date-time":"2026-06-15T15:23:47Z","timestamp":1781537027000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["TDP\u201043 Aggregation: The Healthy\u2010Toxic Balance of the Prion\u2010Like Domain"],"prefix":"10.1002","volume":"13","author":[{"given":"Luca","family":"Zangrando","sequence":"first","affiliation":[{"name":"Life Science Department University of Trieste  Trieste Italy"},{"name":"Molecular Pathology International Centre for Genetic Engineering and Biotechnology  Trieste 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