10 papers analyzed
These studies suggest that PKC expression impacts phosphorylation by involving PDK1 for stability and activation, regulating various cellular processes, and exhibiting isoform-specific phosphorylation effects.
Protein kinase C (PKC) is a family of serine/threonine kinases involved in various cellular processes, including proliferation, differentiation, and apoptosis. Phosphorylation is a critical regulatory mechanism for PKC activity, influencing its stability, localization, and function. This synthesis explores the impact of PKC expression on phosphorylation, drawing insights from multiple research studies.
Role of PDK1 in PKC Phosphorylation and Stability:
PKC Isoforms and Substrate Specificity:
PKC and NADPH Oxidase Activation:
PKC-δ and Glutamine Synthetase Expression:
PKC-η and Cell Cycle Regulation:
Cross-regulation of PKC Isoforms:
PKC-θ in T Cell Signaling:
The expression and phosphorylation of PKC isoforms are intricately regulated by various kinases, including PDK1. This regulation is crucial for the stability, localization, and functional specificity of PKC isoforms. Different PKC isoforms exhibit unique substrate specificities and play distinct roles in cellular processes such as NADPH oxidase activation, glutamine synthetase expression, cell cycle regulation, and T cell signaling. Understanding these mechanisms provides valuable insights into the diverse functions of PKC in cellular physiology.
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