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Literature summary for 2.7.11.26 extracted from

  • Lin, Y.T.; Cheng, J.T.; Liang, L.C.; Ko, C.Y.; Lo, Y.K.; Lu, P.J.
    The binding and phosphorylation of Thr231 is critical for Taus hyperphosphorylation and functional regulation by glycogen synthase kinase 3beta (2007), J. Neurochem., 103, 802-813.
    View publication on PubMed
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Application

Application Comment Organism
additional information phosphorylation of T231 by GSK3beta may play an important role in tau’s hyperphosphorylation and functional regulation Mus musculus

Cloned(Commentary)

Cloned (Comment) Organism
His-tagged GSK3beta expressed in Escherichia coli BL21, into pEGFP vector and N18 cells transiently transfected Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
additional information N-terminus negatively regulates tau phosphorlyation by blocking GSK3beta access, local conformational change induced by T231 phosphorylation is required for the phosphorylation of the C-terminus and hyperphosphorylation of tau Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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-
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Purification (Commentary)

Purification (Comment) Organism
-
 Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
additional information N18 cell, hyperphosphorylation reduces tau’s ability to promote tubulin assembly and to form bundles Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + protein tau T231 is the primary phosphorylation site for GSK3beta, the tau227-237 (AVVRTPPKSPS) derived from tau containing T231P232 motif is the GSK3beta binding site with high affinity (Kd = 0.00082 mmol/L), tau mutant T231A completely abolishes tau phosphorylation by GSK3beta Mus musculus ADP + protein tau phosphate
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Synonyms

Synonyms Comment Organism
glycogen synthase kinase 3beta
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 Mus musculus
GSK3beta
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 Mus musculus
tau protein kinase I
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 Mus musculus