Polymerization of tau peptides into fibrillar structures. The effect of FTDP-17 mutations.
The peptides corresponding to the four repeats found in the microtubule binding region of tau protein were synthesized and their ability for self-aggregation in presence of heparin or chondroitin sulfate was measured. Mainly, only the peptide containing the third tau repeat is able to form polymers in a high proportion. Additionally, the peptide containing the second repeat aggregates with a very low efficiency. However, when this peptide contains the mutation (P301L), described in a fronto temporal dementia, it is able to form polymers at a higher extent. Finally, it is suggested to have a role for the first and fourth tau repeats. It could be to decrease the ability of the third tau repeat for self-aggregation in the presence of heparin.
Arrasate
M
M
Centro de Biología Molecular Severo Ochoa, Facultad de Ciencias UAM, Cantoblanco, Madrid, Spain.
Pérez
M
M
Armas-Portela
R
R
Avila
J
J
D000595:Amino Acid Sequence; D000818:Animals; D019281:Dimerization; D008870:Microtubules / Q000737:chemistry; D008969:Molecular Sequence Data; D009154:Mutation; D017510:Protein Folding; D016875:tau Proteins / Q000737:chemistry* / Q000235:genetics
D016875:tau Proteins