PDPK1 stands for 3-phosphoinositide-dependent protein kinase 1. PDPK1 functions downstream of PI3K through PDPK1's interaction with membrane phospholipids including phosphatidylinositols, phosphatidylinositol (3,4)-bisphosphate and …

2022年4月6日 · 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...

Here we describe the expression and function of a HIF-1-regulated protein pyruvate dehydrogenase kinase-1 (PDK-1) in head and neck squamous cancer (HNSCC). Using RNAi to downregulate hypoxia-inducible PDK-1, we found that lactate and pyruvate excretion after 16–48 h of hypoxia was suppressed to normoxic levels.

2024年12月25日 · 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. Among its related pathways are Regulation of pyruvate metabolism and ESR-mediated signaling.

PDK1 (3-Phosphoinositide-dependent kinase 1) is a key member of the AGC protein kinase family. It plays an important role in a variety of cellular functions, leading to the activation of the PI3K signaling pathway, an event often associated with the onset and progression of several human cancers.

Protein 3-phosphoinositide-dependent protein kinase-1 (PDK-1) As a member of AGC kinases family, PDK-1, a protein of 556 amino acids, is composed of serine and threonine kinases. The catalytic domain of these serine and threonine kinases show a sequential similarity with cAMP-dependent protein kinase 1 (PKA), cGMP-dependent protein kinase (PKG ...

2024年12月25日 · PDPK1 (3-Phosphoinositide Dependent Protein Kinase 1) is a Protein Coding gene. Diseases associated with PDPK1 include Intestinal Obstruction and Erythrokeratodermia Variabilis Et Progressiva 6. Among its related pathways are …

Here we explore the subcellular location of the PDK-1-mediated phos-phorylation of conventional PKCs, and we address whether this phosphorylation is regulated by phospho-inositide 3-kinase.

PDK1 is the only enzyme capable of phosphorylating the 3rd serine site. When the thiamine pyrophosphatase (TPP) coenzyme is bound, the rates of phosphorylation by all four isozymes are drastically affected; specifically, the incorporation of phosphate groups by PDK1 into sites 2 and 3 is significantly reduced. [8]

Nucleus-located PDK1 regulates growth, invasion and migration of breast cancer cells. These findings highlight the potential use of PGK1 mRNA level, PGK1 promoter hypomethylation, and PGK1 pS203 and PDHK1 pT338 levels as biomarkers for cancer progression and prognosis, and the promising significance of PGK1 as a target in cancer treatment.