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Selective loss of glycogen synthase kinase‐3α in birds reveals distinct roles for GSK‐3 isozymes in tau phosphorylation
Author(s) -
Alon Lina Tsaadon,
Pietrokovski Shmuel,
Barkan Shay,
Avrahami Limor,
Kaidanovich-Beilin Oksana,
Woodgett James R.,
Barnea Anat,
Eldar-Finkelman Hagit
Publication year - 2011
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/j.febslet.2011.03.025
Subject(s) - isozyme , gsk 3 , phosphorylation , biology , glycogen synthase , gsk3b , gene , knockout mouse , kinase , glycogen , biochemistry , atp synthase , gene knockout , microbiology and biotechnology , enzyme
Mammalian glycogen synthase kinase‐3 (GSK‐3), a critical regulator in neuronal signaling, cognition, and behavior, exists as two isozymes GSK‐3α and GSK‐3β. Their distinct biological functions remains largely unknown. Here, we examined the evolutionary significance of each of these isozymes. Surprisingly, we found that unlike other vertebrates that harbor both GSK‐3 genes, the GSK‐3α gene is missing in birds. GSK‐3‐mediated tau phosphorylation was significantly lower in adult bird brains than in mouse brains, a phenomenon that was reproduced in GSK‐3α knockout mouse brains. Tau phosphorylation was detected in brains from bird embryos suggesting that GSK‐3 isozymes play distinct roles in tau phosphorylation during development. Birds are natural GSK‐3α knockout organisms and may serve as a novel model to study the distinct functions of GSK‐3 isozymes.