14-3-3 Proteins and protein phosphatases are not reduced in tau-deficient mice

Katsunori Fujio, Mahito Sato, Takefumi Uemura, Takashi Sato, Reiko Sato-Harada, Akihiro Harada

Research output: Contribution to journalArticlepeer-review

28 Scopus citations

Abstract

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-3β, 14-3-3ζ, 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.

Original languageEnglish
Pages (from-to)1049-1052
Number of pages4
JournalNeuroReport
Volume18
Issue number10
DOIs
StatePublished - Jul 2007
Externally publishedYes

Keywords

  • 14-3-3
  • Alzheimer's disease
  • Glycogen synthase kinase-3β
  • Knockout mice
  • Microtubule-associated protein
  • Protein phosphatase
  • Tau
  • Tauopathies

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