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Target Concepts:
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Query: EC:2.7.11.26 (
GSK
)
6,788
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
In a recent study, we reported that in bovine brain extract,
glycogen synthase kinase-3beta
and tau are parts of an approximately 400-500 kDa microtubule-associated tau phosphorylation complex (Sun, W., Qureshi, H. Y., Cafferty, P. W., Sobue, K., Agarwal-Mawal, A., Neufield, K. D., and Paudel, H. K. (2002) J. Biol. Chem. 277, 11933-11940). In this study, we find that when purified brain microtubules are subjected to Superose 12 gel filtration column chromatography, the dimeric scaffold protein
14-3-3 zeta
co-elutes with the tau phosphorylation complex components tau and GSK3 beta. From gel filtration fractions containing the tau phosphorylation complex,
14-3-3 zeta
, GSK3 beta, and tau co-immunoprecipitate with each other. From extracts of bovine brain, COS-7 cells, and HEK-293 cells transfected with GSK3 beta,
14-3-3 zeta
co-precipitates with GSK3 beta, indicating that GSK3 beta binds to
14-3-3 zeta
. From HEK-293 cells transfected with tau, GSK3 beta, and
14-3-3 zeta
in different combinations, tau co-immunoprecipitates with GSK3 beta only in the presence of
14-3-3 zeta
. In vitro, approximately 10-fold more tau binds to GSK3 beta in the presence of than in the absence of
14-3-3 zeta
. In transfected HEK-293 cells,
14-3-3 zeta
stimulates GSK3 beta-catalyzed tau phosphorylation in a dose-dependent manner. These data indicate that in brain, the
14-3-3 zeta
dimer simultaneously binds and bridges tau and GSK3 beta and stimulates GSK3 beta-catalyzed tau phosphorylation.
...
PMID:14-3-3 connects glycogen synthase kinase-3 beta to tau within a brain microtubule-associated tau phosphorylation complex. 1255 48