Differential distribution in white and grey matter of tau phosphoisoforms containing four tubulin-binding motifs.
The microtubule-associated protein tau has been isolated and purified from both white and grey brain matter. Tau isoforms were fractionated, based on their different phosphate contents, by iron-chelating affinity chromatography. Differences were observed in the proportions of phosphorylated isoforms of tau protein (containing four tubulin-binding motifs) present in white and grey matter. In white matter, isoforms containing four tubulin-binding motifs are mainly present in a phosphorylated form. Thus there appears to be a correlation between the modification, by phosphorylation, of some sites in the tau molecule and the subcellular localization (axonal or somatodendritic compartments) of the modified isoforms.
de Ancos
J G
JG
Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Facultad de Ciencias, Universidad Autónoma de Madrid, Spain.
Avila
J
J
D000469:Alkaline Phosphatase; D001665:Binding Sites; D002540:Cerebral Cortex / Q000737:chemistry*; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D007502:Iron Chelating Agents; D010750:Phosphoproteins / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D010766:Phosphorylation; D014404:Tubulin / Q000378:metabolism*; D016875:tau Proteins / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism
D007502:Iron Chelating Agents; D010750:Phosphoproteins; D014404:Tubulin; D016875:tau Proteins; D000469:Alkaline Phosphatase