Abstract:
:Coding region and intronic mutations in the gene for microtubule-associated protein tau cause frontotemporal dementia and Parkinsonism linked to chromosome 17 (FTDP-17). Most coding region mutations effect a reduced ability of tau protein to interact with microtubules and lead to the formation of a filamentous pathology made of hyperphosphorylated tau. Here we show that trimethylamine N-oxide (TMAO) restores the ability of tau with FTDP-17 mutations to promote microtubule assembly. To mimic phosphorylation, serine and threonine residues in tau were singly or multiply mutated to glutamic acid, resulting in a reduced ability of tau to promote microtubule assembly. With the exception of the most heavily substituted protein (27 glutamic acid residues), TMAO increased the ability of mutant tau to promote microtubule assembly. However, it had no significant effect on heparin-induced assembly of tau into filaments.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Smith MJ,Crowther RA,Goedert Mdoi
10.1016/s0014-5793(00)02169-4keywords:
subject
Has Abstractpub_date
2000-11-10 00:00:00pages
265-70issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(00)02169-4journal_volume
484pub_type
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