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• W2023333640 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." @default.
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• W2023333640 date "1999-07-01" @default.
• W2023333640 modified "2023-09-24" @default.
• W2023333640 title "Disulfide-Cross-Linked Tau and MAP2 Homodimers Readily Promote Microtubule Assembly" @default.
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• W2023333640 doi "https://doi.org/10.1006/mcbr.1999.0153" @default.
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