Protein Kinase C Epsilon
Protein Kinase C Epsilon - Related Videos
02:54
Protein Kinases and Phosphatases
0 Views •
2020
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven. Protein kinases Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
02:54
Protein Kinases and Phosphatases
0 Views •
2023
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven. Protein kinases Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
15:43
Assessment of Mitochondrial Functions and Cell Viability in Renal Cells Overexpressing Protein Kinase C Isozymes
0 Views •
Cited by 5 •
2013
The effects of activation of protein kinase C (PKC) isozymes on mitochondrial functions associated with respiration and oxidative phosphorylation and on cell viability are described. The approach adapts adenoviral technique to selectively overexpress PKC isozymes in primary cell culture and a variety of assays to determine mitochondrial functions and energy status of the cell.
08:05
Assaying Protein Kinase Activity with Radiolabeled ATP
0 Views •
Cited by 15 •
2017
Protein kinases are highly evolved signaling enzymes and scaffolds that are critical for inter- and intracellular signal transduction. We present a protocol for measuring kinase activity through the use of radiolabeled adenosine triphosphate ([γ-32P] ATP), a reliable method to aid in elucidation of cellular signaling regulation.
06:37
Visualizing Protein Kinase A Activity in a Mouse Using Two-Photon Fluorescence Lifetime Imaging Microscopy
0 Views •
2025
Source: Jongbloets, B. C., et al. Visualizing Protein Kinase A Activity In Head-fixed Behaving Mice Using In Vivo Two-photon Fluorescence Lifetime Imaging Microscopy. J. Vis. Exp. (2019) This video demonstrates a two-photon fluorescence lifetime imaging microscopy procedure for visualizing protein kinase A activity in head-fixed, behaving mice during enforced locomotion.
FAQs
These lipid signals provide the activating conditions that PKCε requires while calcium remains unnecessary. Their presence promotes activation and supports movement of the kinase to particular cellular compartments. This calcium-independent response distinguishes PKCε from protein kinase C isoforms that depend on calcium and helps explain how distinct signaling conditions produce isoform-specific cellular effects.
Activation alone does not determine which substrates PKCε can modify. After activation, translocation places the kinase in selected cellular compartments, bringing it closer to particular target proteins. This spatial organization helps connect lipid-generated signals with localized changes in phosphorylation, allowing PKCε to influence processes such as cytoskeletal organization, cell survival, and gene expression.
Phosphorylation by PKCε can affect several biologically important processes, including cell survival, cytoskeletal organization, inflammation, and gene expression. The outcome depends on the signaling context and the cellular targets reached after translocation. Consequently, altered PKCε signaling may influence both structural features of cells and broader programs governing stress responses and cellular behavior.
Research examines PKCε as part of signaling responses associated with cardiac protection and cellular stress. Its activation, compartmental movement, and effects on target proteins provide a framework for connecting upstream lipid signals with protective or adaptive cellular outcomes. This makes the isoform relevant for clarifying how cells respond when physiological conditions place them under stress.
PKCε attracts attention in nervous system studies because its signaling can affect cellular processes relevant to neural function. In cancer research, the same pathway is examined in relation to cell survival, inflammation, cytoskeletal organization, and gene expression, all of which can contribute to altered cellular behavior. These applications show why its effects must be interpreted by biological context.
Investigating PKCε can reveal how one protein kinase links lipid signals to compartment-specific phosphorylation and downstream cellular responses. Such knowledge supports efforts to distinguish its functions from those of related protein kinase C isoforms. The long-term research goal is to inform isoform-selective therapeutic strategies while accounting for roles in cardiac protection, nervous system function, cancer progression, and stress responses.