Premium
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
Author(s) -
Goedert M.,
Jakes R.,
Qi Z.,
Wang J. H.,
Cohen P.
Publication year - 1995
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1995.65062804.x
Subject(s) - c raf , protein kinase a , phosphatase , cyclin dependent kinase 2 , mitogen activated protein kinase kinase , gsk 3 , phosphorylation , map2k7 , cyclin dependent kinase 1 , dusp6 , biochemistry , kinase , ask1 , map kinase kinase kinase , protein phosphorylation , protein phosphatase 2 , protein phosphatase 1 , autophagy related protein 13 , chemistry , biology , cell cycle , cell
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.