Cargando…
Disruption of tubulin-alpha4a polyglutamylation prevents aggregation of hyper-phosphorylated tau and microglia activation in mice
Dissociation of hyper-phosphorylated Tau from neuronal microtubules and its pathological aggregates, are hallmarks in the etiology of tauopathies. The Tau-microtubule interface is subject to polyglutamylation, a reversible posttranslational modification, increasing negative charge at tubulin C-termi...
Autores principales: | Hausrat, Torben Johann, Janiesch, Philipp C., Breiden, Petra, Lutz, David, Hoffmeister-Ullerich, Sabine, Hermans-Borgmeyer, Irm, Failla, Antonio Virgilio, Kneussel, Matthias |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9300677/ https://www.ncbi.nlm.nih.gov/pubmed/35858909 http://dx.doi.org/10.1038/s41467-022-31776-5 |
Ejemplares similares
-
Spastin depletion increases tubulin polyglutamylation and impairs kinesin-mediated neuronal transport, leading to working and associative memory deficits
por: Lopes, André T., et al.
Publicado: (2020) -
Tubulin polyglutamylation stimulates spastin-mediated microtubule severing
por: Lacroix, Benjamin, et al.
Publicado: (2010) -
Reduced tubulin polyglutamylation suppresses flagellar shortness in Chlamydomonas
por: Kubo, Tomohiro, et al.
Publicado: (2015) -
Tubulin polyglutamylation differentially regulates microtubule‐interacting proteins
por: Genova, Mariya, et al.
Publicado: (2023) -
Severe ciliopathy-related phenotypes in mice with dysregulation of tubulin polyglutamylation
por: Ikegami, K, et al.
Publicado: (2012)