14-3-3 proteins and protein phosphatases are not reduced in tau-deficient mice.
Tau is an axonal microtubule-associated protein, whose dysfunction causes neurodegenerative diseases such as Alzheimer's disease and other tauopathies. Earlier studies have shown the interactions of tau with glycogen synthase kinase-3beta, 14-3-3zeta, protein phosphatase 1 and protein phosphatase 2A. In this study, we compared the amounts of these tau-interacting proteins in brain microtubule-enriched fractions from wild-type and tau-deficient mice. Contrary to our expectation, we detected no difference in the amount of these proteins between wild-type and tau-deficient mice. Our findings indicate that only a small portion of tau-interacting proteins are bound to tau in vivo, and suggest the existence of other scaffolding proteins. We propose that tau-deficient mice are an ideal system for confirming the function of tau-interacting proteins.
Fujio
Katsunori
K
Laboratory of Molecular Traffic, Department of Molecular and Cellular Biology, Institute for Molecular and Cellular Regulation, Gunma University, Japan.
Sato
Mahito
M
Uemura
Takefumi
T
Sato
Takashi
T
Sato-Harada
Reiko
R
Harada
Akihiro
A
D048948:14-3-3 Proteins / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000378:metabolism; D001923:Brain Chemistry; D051379:Mice; D018345:Mice, Knockout; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D054645:Protein Phosphatase 1; D054648:Protein Phosphatase 2; D016875:tau Proteins / Q000172:deficiency*
D048948:14-3-3 Proteins; D016875:tau Proteins; D010749:Phosphoprotein Phosphatases; D054645:Protein Phosphatase 1; D054648:Protein Phosphatase 2