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Differential effects of apolipoprotein E isoforms on phosphorylation at specific sites on tau by glycogen synthase kinase‐3β identified by nano‐electrospray mass spectrometry
Author(s) -
Gibb Graham M,
Pearce Janice,
Betts Joanna C,
Lovestone Simon,
Hoffmann Michael M,
Maerz Winfried,
Blackstock Walter P,
Anderton Brian H
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02196-7
Subject(s) - gsk 3 , phosphorylation , glycogen synthase , phosphopeptide , gene isoform , apolipoprotein e , chemistry , kinase , biochemistry , gsk3b , microbiology and biotechnology , biology , gene , medicine , disease
Previously published data have shown an allele‐specific variation in the in vitro binding of apolipoprotein E (apoE) to tau, which prompted the hypothesis that apoE binding may protect tau from phosphorylation, apoE3 being more efficient than apoE4. We have, therefore, investigated the effects of apoE on tau phosphorylation in vitro by the proline‐directed kinase, glycogen synthase kinase (GSK)‐3β. The phosphopeptide maps of tau alone, of tau with apoE3 and of tau with apoE4 were very similar. When apoE2 was present a further four spots were evident. Additionally, of the 15 peptides phosphorylated in the presence or absence of apoE, subtle differences, some isoform‐specific, in the relative amounts of phosphorylation were observed.