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Suggest that CTMP may therefore play a critical role in mitochondrial-mediated apoptosis in lung cancer cells.
Data show low or moderate methylation was found in seven selected genes BAD, BBC3 (show BBC3 Proteins), CAV1 (show CAV1 Proteins), CDK2AP1 (show CDK2AP1 Proteins), NPM1 (show NPM1 Proteins), PRKCDBP (show PRKCDBP Proteins) and THEM4.
CTMP induces translocation of Akt (show AKT1 Proteins) to the membrane and thereby increases the level of Akt (show AKT1 Proteins) phosphorylation. As a result, CTMP enhances various cellular activities that are principally mediated by the PI3-kinase (show PIK3CA Proteins)/Akt (show AKT1 Proteins) pathway.
Proper maturation of CTMP is essential for its pro-apoptotic function. CTMP delays PKB (show AKT1 Proteins) phosphorylation following cell death induction, suggesting that CTMP regulates apoptosis via inhibition of PKB (show AKT1 Proteins).
Phosphorylation on Ser37/Ser38 of CTMP is important for the prevention of mitochondrial localization of CTMP, eventually leading to cell death by binding to heat shock protein 70 (show HSP70 Proteins).
Results suggest that Akt (show AKT1 Proteins) is phosphorylated and translocated to nucleus after traumatic brain injury (TBI (show TBPL1 Proteins)) to exert neuroprotective effects; however, CTMP is simultaneously triggered to inhibit the phosphorylation of Akt (show AKT1 Proteins)
Protein kinase B (PKB) is a major downstream target of receptor tyrosine kinases that signal via phosphatidylinositol 3-kinase. Upon cell stimulation, PKB is translocated to the plasma membrane, where it is phosphorylated in the C-terminal regulatory domain. The protein encoded by this gene negatively regulates PKB activity by inhibiting phosphorylation. Transcription of this gene is commonly downregulated in glioblastomas.
thioesterase superfamily member 4
, acyl-coenzyme A thioesterase THEM4
, C-terminal modulator protein
, acyl-CoA thioesterase THEM4
, carboxyl-terminal modulator protein