| First Author | Fujio K | Year | 2007 |
| Journal | Neuroreport | Volume | 18 |
| Issue | 10 | Pages | 1049-52 |
| PubMed ID | 17558294 | Mgi Jnum | J:123734 |
| Mgi Id | MGI:3719342 | Doi | 10.1097/WNR.0b013e32818b2a0b |
| Citation | Fujio K, et al. (2007) 14-3-3 proteins and protein phosphatases are not reduced in tau-deficient mice. Neuroreport 18(10):1049-52 |
| abstractText | 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. |
