The BioGRID | PUBLICATION VIEW

	Mol. Cell Biol. Res. Commun. Jul (1999); 2(1):71-6
Disulfide-cross-linked tau and MAP2 homodimers readily promote microtubule assembly.
Di Noto L, DeTure MA, Purich DL
Department of Biochemistry and Molecular Biology, University of Florida College of Medicine, Health Science Center, Gainesville 32610-0245, USA.
Abstract: The neuronal proteins Tau and MAP2 use homologous C-terminal MT-binding regions (MTBRs) to interact with microtubules, F-actin, and intermediate filaments. Although Tau-MTBR is the principal component of pronase-treated Alzheimer paired helical filaments, both Tau and MAP2 form filaments in vitro from disulfide-linked homodimers. That the critical thiol lies within a domain needed for MT binding raised the question: Does disulfide formation block Tau-Tau or MAP2-MAP2 dimer binding to microtubules, thereby acting to divert dimers toward filament formation? We now report that cross-linked Tau and MAP2 homodimers readily promote tubulin polymerization and that monomer and dimer affinity for MTs is surprisingly similar. Therefore, disulfide cross-bridging into homodimers is unlikely to be a drive force for filament formation in Alzheimer's disease.
[PUBMED: 10527895]