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Neurobiology
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- NeurobiologyOpen Access
Isoform-independent and -dependent phosphorylation of microtubule-associated protein tau in mouse brain during postnatal development
Journal of Biological ChemistryVol. 293Issue 5p1781–1793Published online: December 1, 2017- Dilina Tuerde
- Taeko Kimura
- Tomohiro Miyasaka
- Kotaro Furusawa
- Aki Shimozawa
- Masato Hasegawa
- and others
Cited in Scopus: 31Tau is a microtubule (MT)-associated protein that regulates MT dynamics in the axons of neurons. Tau binds to MTs via its C-terminal MT-binding repeats. There are two types of tau, those with three (3R) or four (4R) MT-binding repeats; 4R tau has a stronger MT-stabilizing activity than 3R tau. The MT-stabilizing activity of tau is regulated by phosphorylation. Interestingly, both the isoform and phosphorylation change at the time of neuronal circuit formation during postnatal development; highly phosphorylated 3R tau is replaced with 4R tau, which is less phosphorylated.