Tau aggregation

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dc.contributor.authorDomene-Serrano, Indalo
dc.contributor.authorSanta-María, Ismael
dc.contributor.authorHernandez, Felix
dc.contributor.authorAvila, Jesús
dc.contributor.departmentBiología Celular e Histología
dc.date.accessioned2026-01-07T11:48:42Z
dc.date.available2026-01-07T11:48:42Z
dc.date.issued2026
dc.description.abstractMicrotubule-associated protein tau is predominantly expressed in neurons in the form of multiple isoforms generated by alternative splicing. These isoforms differ in the presence of either three or four microtubule-binding repeats. These binding regions not only regulate tau’s interaction with microtubules but are also critically involved in its pathological self-aggregation. Such aggregates are a defining feature of a group of neurodegenerative disorders collectively referred to as tauopathies. In this work, we examine the mechanisms underlying tau self-aggregation, the molecular and cellular factors that drive this process, and the structural features of tau aggregates. Aggregates composed of isoforms with three versus four microtubule-binding repeats display distinct morphologies, which serve as pathological hallmarks for different tauopathies. Finally, we discuss potential therapeutic strategies aimed at preventing or promoting the clearance of tau aggregates.
dc.formatapplication/pdf
dc.format.extent9
dc.identifier.citationHistology and Histopathology, vol.41, nº2(2026)173-181
dc.identifier.doihttps://doi.org/10.14670/HH-18-961
dc.identifier.eissn1699-5848
dc.identifier.issn0213-3911
dc.identifier.urihttp://hdl.handle.net/10201/183709
dc.languageeng
dc.publisherUniversidad de Murcia, Departamento de Histología e Histopatología
dc.relationEste trabajo ha sido financiado por subvenciones del Ministerio de Ciencia español: PID2020-113204GB-I00 (F.H.) y PID2021-123859OB-100 de MCIN/AEI/10.13039/501100011033/ FEDER, UE (J.A.)
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International*
dc.rights.accessRightsinfo:eu-repo/semantics/openAccess
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectTau protein
dc.subjectTau aggregation
dc.subjectOligomer
dc.subjectFilaments
dc.subjectRegulatory factors
dc.subject.odsNo relacionado con ningún objetivo de desarrollo sostenible
dc.titleTau aggregation
dc.typeinfo:eu-repo/semantics/article
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Histology and histopathology, Vol.41, Nº2, (2026)