Structural stability of paired helical filaments requires microtubule-binding domains of tau: a model for self-association.
Neuron
; 6(5): 717-28, 1991 May.
Article
en En
| MEDLINE
| ID: mdl-1709023
ABSTRACT
Highly purified and SDS-soluble paired helical filaments (PHFs) were immunogold labeled and immunoblotted with antibodies to tau Tau 14 (N-terminal half), AH-1 (microtubule-binding domain), and Tau 46 (C-terminal end). The main component of PHFs was modified tau of 68, 64, and 60 kd, also called A68 or PHF-tau. Trypsin digestion reduced the maximum width of PHFs by 10%-20%, increased aggregation of filaments, and abolished the binding of Tau 14, but had no effect on the binding of AH-1. The smallest tau-reactive tryptic fragments were 13 and 7-8 kd, positive with AH-1, and negative with Tau 46. Our results and the model of Crowther and Wischik suggest that by self-association and anti-parallel arrangement of the microtubule-binding domains, PHF-tau forms the backbone of PHFs.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteínas Asociadas a Microtúbulos
/
Microtúbulos
/
Proteínas del Tejido Nervioso
/
Neurofibrillas
Tipo de estudio:
Risk_factors_studies
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Neuron
Asunto de la revista:
NEUROLOGIA
Año:
1991
Tipo del documento:
Article