TTK: A Potential Drug Target and Biomarker for Pyruvate Kinase-Driven Diseases

Target Name: TTK

NCBI ID: G7272

TTK: A Potential Drug Target and Biomarker for Pyruvate Kinase-Driven Diseases

Pyruvate kinase (PK) is an enzyme that plays a crucial role in the metabolism of pyruvate, a crucial intermediate step in the citric acid cycle. PK is a protein that catalyzes the transfer of a phosphate group from a Pyruvate molecule to a threonine molecule, which activates the citric acid cycle and ultimately generates energy in the form of ATP. PK is also involved in the regulation of cellular processes, including cell growth, differentiation, and stress resistance. Therefore, alterations in PK activity or function have been implicated in a wide range of diseases, including cancer, neurodegenerative diseases, and metabolic disorders.

TTK, or Pyruvate Threonine Kinase, is a protein that is highly conserved across various species, including humans. It is a 21-kDa protein that is localized to the endoplasmic reticulum (ER) and plays a critical role in the regulation of PK activity.TTK is composed of 115 amino acid residues and has a calculated pI of 9.95 nM. It consists of a catalytic active site, a regulatory region, and a C-terminal region that is involved in protein-protein interactions.

TTK functions as a negative regulator of PK, which means that it inhibits the activity of PK. This is achieved by a unique mechanism that involves a unique protein-protein interaction between TTK and PK. Specifically, TTK contains a cal sequence, which is a conserved motif that is involved in protein-protein interactions. This motif is present in the catalytic active site of PK, allowing it to interact with TTK and inhibit its activity.

TTK has been extensively studied for its role in PK regulation, and several studies have identified its involvement in various cellular processes, including cell growth, apoptosis, and stress resistance. For example, studies have shown that TTK is involved in the regulation of cell cycle progression, and that it promotes the G1 phase by inhibiting the activity of the cell cycle kinetic protein, p21. Additionally,TTK has been shown to play a role in the regulation of apoptosis, as it has been shown to induce cell death in response to various stressors, including starvation, UV radiation, and reactive oxygen species (ROS).

TTK has also been shown to be involved in the regulation of various metabolic processes, including glycolysis, the citric acid cycle, and the regulation of amino acid metabolism. For example, studies have shown that TTK is involved in the regulation of glucose metabolism, as it has been shown to play a role in the upregulation of GLUT1, a glucose transporter. Additionally,TTK has been shown to be involved in the regulation of amino acid metabolism, as it has been shown to play a role in the regulation of protein synthesis and degradation.

In conclusion, TTK is a protein that is highly conserved across various species and has been shown to play a critical role in the regulation of PK activity. Its involvement in various cellular processes, including cell growth, apoptosis, and stress resistance, makes it an attractive drug target and a potential biomarker for a wide range of diseases. Further studies are needed to fully understand the mechanisms of TTK's role in PK regulation and its potential as a drug target.

Protein Name: TTK Protein Kinase

Functions: Phosphorylates proteins on serine, threonine, and tyrosine (PubMed:18243099, PubMed:29162720). Probably associated with cell proliferation (PubMed:18243099). Phosphorylates MAD1L1 to promote mitotic checkpoint signaling (PubMed:29162720). Essential for chromosome alignment by enhancing AURKB activity (via direct CDCA8 phosphorylation) at the centromere, and for the mitotic checkpoint (PubMed:18243099)

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