Literature summary for 2.7.11.22 extracted from

Sengupta, A.; Novak, M.; Grundke-Iqbal, I.; Iqbal, K.
Regulation of phosphorylation of tau by cyclin-dependent kinase 5 and glycogen synthase kinase-3 at substrate level (2006), FEBS Lett., 580, 5925-5933.

Search for more literature for 2.7.11.22

Application

Application	Comment	Organism
medicine	combined action of the two protein kinases cdk5 and GSK-3 may be involved in the abnormal hyperphosphorylation of microtubule associated tau protein in Alzheimer disease	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
expressed from Escherichia coli as GST fusion protein	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
by immunoprecipitation	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + tau protein	phosphorylation at Ser235 by cdk5 primes phosphorylation at Thr231 by GSK-3alpha/beta. Tau protein isoforms with the two N-terminal inserts s4L and s3L are more favorable substrates than tau protein isoforms without the inserts. Thr231 is phosphorylated ca. 50% more in free tau protein than in microtubule-bound one	Homo sapiens	ADP + phosphorylated tau protein	-	?

Synonyms

Synonyms	Comment	Organism
Cdk5	-	Homo sapiens
cyclin-dependent kinase 5	-	Homo sapiens

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Release 2023.1 (January 2023)