Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/252132
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | The FTDP-17-linked mutation R406W abolishes the interaction of phosphorylated tau with microtubules |
Autor: | Pérez, Mar CSIC ORCID; Lim, Filip CSIC ORCID; Arrasate, Montserrat; Ávila, Jesús CSIC ORCID | Fecha de publicación: | 2000 | Editor: | Wiley-VCH | Citación: | Journal of Neurochemistry 74(6): 2583-2589 (2000) | Resumen: | The recent finding that several point mutations in the gene encoding for the microtubule-binding protein tau correlate with neurological disorders has heightened interest in the mechanisms of destabilization of this protein. In this study the functional consequences of the tau mutation R406W on the interaction of the protein with microtubules have been analyzed. Mutated tau is less phosphorylated than its normal counterpart at serines 396 and 404. Furthermore, the phosphorylated mutant protein is unable to bind to microtubules, and, as a consequence, microtubules assembled after transient nocodazole treatment in the presence of this tau variant contain only unmodified tau and appear to form more and longer bundles than those assembled in the presence of wild-type tau. We propose that phosphorylated tau, unbound to microtubules, could accumulate in the cytoplasm. | Versión del editor: | https://doi.org/10.1046/j.1471-4159.2000.0742583.x | URI: | http://hdl.handle.net/10261/252132 | DOI: | 10.1046/j.1471-4159.2000.0742583.x | ISSN: | 0022-3042 |
Aparece en las colecciones: | (CBM) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
accesoRestringido.pdf | 59,24 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
61
checked on 12-abr-2024
WEB OF SCIENCETM
Citations
61
checked on 22-feb-2024
Page view(s)
42
checked on 19-abr-2024
Download(s)
9
checked on 19-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.