regulation of tau-protein kinase activity

Definition

Target type: biologicalprocess

Any process that modulates the frequency, rate or extent of tau-protein kinase activity. [GO_REF:0000059, GOC:sjp, GOC:TermGenie, PMID:15897157, PMID:22986780]

Tau-protein kinase (TPK) activity is tightly regulated to ensure proper neuronal function and prevent the formation of neurofibrillary tangles, a hallmark of neurodegenerative diseases like Alzheimer's disease. This intricate regulation involves a complex interplay of multiple factors, including phosphorylation, dephosphorylation, ubiquitination, and interactions with other proteins.

* **Phosphorylation:** TPK activity is modulated by phosphorylation events, which can either activate or inhibit its kinase activity. Kinases like cyclin-dependent kinase 5 (CDK5) and glycogen synthase kinase-3β (GSK-3β) can phosphorylate TPK at specific residues, leading to its activation. Conversely, phosphatases such as protein phosphatase 2A (PP2A) can dephosphorylate these sites, inhibiting TPK activity.
* **Dephosphorylation:** Dephosphorylation plays a crucial role in regulating TPK activity. Phosphatases, particularly PP2A, remove phosphate groups from specific residues on TPK, leading to a decrease in its kinase activity.
* **Ubiquitination:** TPK can be ubiquitinated, a process that marks it for degradation by the proteasome. This mechanism helps to regulate the levels of active TPK within the cell.
* **Protein Interactions:** TPK interacts with various proteins that influence its activity. For example, TPK can bind to microtubules, providing a platform for its phosphorylation activity. Specific protein-protein interactions can also modulate TPK localization and activity.

The intricate balance of these regulatory mechanisms ensures that TPK activity remains within a tight range, preventing aberrant phosphorylation of tau protein and the formation of neurofibrillary tangles. Disruptions in this delicate equilibrium can lead to the accumulation of hyperphosphorylated tau, contributing to the pathogenesis of neurodegenerative diseases.'
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Proteins (1)

Compounds (2)