Tau-protein kinase

tau-protein kinase
Identifiers
EC no.	2.7.11.26
CAS no.	111694-09-8
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

In enzymology, a tau-protein kinase (EC 2.7.11.26) is an enzyme that catalyzes the chemical reaction

ATP + tau protein ${\displaystyle \rightleftharpoons }$ ADP + O-phospho-tau-protein

Thus, the two substrates of this enzyme are ATP and tau protein, whereas its two products are ADP and O-phospho-tau-protein.

This enzyme belongs to the family of transferases, specifically, those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). This enzyme participates in 14 metabolic pathways: erbb signaling pathway, cell cycle, wnt signaling pathway, hedgehog signaling pathway, axon guidance, focal adhesion, b cell receptor signaling pathway, insulin signaling pathway, melanogenesis, alzheimer's disease, colorectal cancer, endometrial cancer, prostate cancer, and basal cell carcinoma.

Nomenclature

The systematic name of this enzyme class is ATP:[tau-protein] O-phosphotransferase. Other names in common use include ATP:tau-protein O-hosphotransferase, brain protein kinase PK40erk, cdk5/p20, CDK5/p23, glycogen synthase kinase-3beta, GSK, protein tau kinase, STK31, tau kinase, [tau-protein] kinase, tau-protein kinase I, tau-protein kinase II, tau-tubulin kinase, TPK, TPK I, TPK II, and TTK.

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2JDO, 2JDR, and 2UW9.

Examples

Human genes encoding proteins with Tau-protein kinase activity include:

• BRSK1
• BRSK2
• GSK3A
• GSK3B

References

• Ishiguro K, Ihara Y, Uchida T, Imahori K (September 1988). "A novel tubulin-dependent protein kinase forming a paired helical filament epitope on tau". J. Biochem. 104 (3). Tokyo: 319–21. doi:10.1093/oxfordjournals.jbchem.a122465. PMID 2467901.
• Lund ET, McKenna R, Evans DB, Sharma SK, Mathews WR (2001). "Characterization of the in vitro phosphorylation of human tau by tau protein kinase II (cdk5/p20) using mass spectrometry". J. Neurochem. 76 (4): 1221–32. doi:10.1046/j.1471-4159.2001.00130.x. PMID 11181841. S2CID 24005862.
• Takashima A; Mercken, M; Murayama, M; Noguchi, K; Ishiguro, K; Imahori, K; Takashima, A (1998). "Characterization of tau phosphorylation in glycogen synthase kinase-3beta and cyclin dependent kinase-5 activator (p23) transfected cells". Biochim. Biophys. Acta. 1380 (2): 177–82. doi:10.1016/s0304-4165(97)00139-6. PMID 9565682.
• Sugio S, Kohno T, Matsuzaki T (November 2000). "Expression, purification and crystallization of human tau-protein kinase I/glycogen synthase kinase-3beta". Acta Crystallogr. D. 56 (Pt 11): 1464–5. doi:10.1107/S0907444900010386. PMID 11053853.