Protein Phosphatase 2A Is the Major Enzyme in Brain that Dephosphorylates τ Protein Phosphorylated by Proline‐Directed Protein Kinases or Cyclic AMP‐Dependent Protein Kinase

M. Goedert, R. Jakes, Z. Qi, J. H. Wang, P. Cohen

    Research output: Contribution to journalArticlepeer-review

    142 Citations (Scopus)

    Abstract

    Abstract: The paired helical filament (PHF), which makes up the major fibrous component of the neurofibrillary lesions of Alzheimer's disease, is composed of hyperphosphorylated and abnormally phosphorylated microtubule‐associated protein τ. Previous studies have identified serine and threonine residues phosphorylated in PHF‐τ and have shown that τ can be phosphorylated at several of these sites by proline‐directed protein kinases and cyclic AMP‐dependent protein kinase. Here we have investigated which protein phosphatase activities can dephosphorylate recombinant τ phosphorylated with mitogen‐activated protein kinase, glycogen synthase kinase‐3β, neuronal cdc2‐like kinase, or cyclic AMP‐dependent protein kinase. We show that protein phosphatase 2A is by far the major protein phosphatase activity in brain that dephosphorylates τ phosphorylated in this manner.

    Original languageEnglish
    Pages (from-to)2804-2807
    Number of pages4
    JournalJournal of Neurochemistry
    Volume65
    Issue number6
    DOIs
    Publication statusPublished - Dec 1995

    Keywords

    • Dephosphorylation
    • Paired helical filaments
    • Protein phosphatase 2A
    • τ protein

    Fingerprint Dive into the research topics of 'Protein Phosphatase 2A Is the Major Enzyme in Brain that Dephosphorylates τ Protein Phosphorylated by Proline‐Directed Protein Kinases or Cyclic AMP‐Dependent Protein Kinase'. Together they form a unique fingerprint.

    Cite this