PDPK1 is a master kinase, which is crucial for the activation of AKT /PKB and many other AGC kinases including PKC, S6K, SGK. An important role for PDPK1 is in the signaling pathways activated by several growth factors and hormones including insulin signaling.

Mar 30, 2025 · PDK1 (Pyruvate Dehydrogenase Kinase 1) is a Protein Coding gene. Diseases associated with PDK1 include Pyruvate Dehydrogenase E3-Binding Protein Deficiency and Polycystic Kidney Disease 1 With Or Without Polycystic Liver Disease .

Pyruvate dehydrogenase kinase (PDK) can regulate the catalytic activity of pyruvate decarboxylation oxidation via the mitochondrial pyruvate dehydrogenase complex, and it further links glycolysis with the tricarboxylic acid cycle and ATP generation.

PDK1 regulates the progression of esophageal squamous cell carcinoma through metabolic reprogramming. Circular RNA PDK1 targets miR-4731-5p to enhance TNXB expression in ligamentum flavum hypertrophy.

Pyruvate dehydrogenase kinase (also pyruvate dehydrogenase complex kinase, PDC kinase, or PDK; EC 2.7.11.2) is a kinase enzyme which acts to inactivate the enzyme pyruvate dehydrogenase by phosphorylating it using ATP.

Apr 6, 2022 · PDK1 (3-phosphoinositide-dependent kinase 1) is a serine/threonine-protein kinase that plays a central role in regulating cell growth, survival, and proliferation. Knocking out PDK1 in mice...

PDK1 is relevant in a variety of clinical conditions throughout the body. As PDK1 regulates the PDH complex, it has been proven to be an important regulator in certain cells, including the beta cells within the islets of the pancreas.

Mar 1, 2022 · Acute myeloid leukemia remains difficult to treat due to strong genetic heterogeneity between and within individual patients. Here, we show that Pyruvate dehydrogenase kinase 1 (PDK1) acts as...

Jan 4, 2025 · Pyruvate dehydrogenase kinase regulates vascular inflammation in atherosclerosis and increases cardiovascular risk.

PDK1 is a 63 KDa Ser/Thr kinase with carboxyl terminal PH domain that binds with high affinity to PIP3-containing regions of plasma membrane and phosphorylates the colocalised AKT at its threonine 308 residue partially activating it (Mora et al., 2004).