Pi3-kinase Signaling
Pi3-kinase Signaling - Related Videos
06:42
Identifying Kinase Inhibitors that Modulate the Thymocyte Response to Strong TCR Signals
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2025
In this video, we describe a method to identify the small-molecule kinase inhibitors that modulate the apoptosis of self-reactive CD4+CD8+ double-positive immature thymocytes. Apoptosis is induced in the double-positive thymocytes by activating them with anti-CD3- and anti-CD28-coated magnetic beads; this is followed by a small-molecule inhibitor treatment and flow cytometry analysis to detect if the inhibitors modulate the apoptotic marker expression.
11:20
An Integrated System to Remotely Trigger Intracellular Signal Transduction by Upconversion Nanoparticle-mediated Kinase Photoactivation
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Cited by 1 •
2017
In this protocol, caged protein kinase A (PKA), a cellular signal transduction bioeffector, was immobilized on a nanoparticle surface, microinjected into the cytosol, and activated by the upconverted UV light from near-infrared (NIR) irradiation, inducing downstream stress fiber disintegration in the cytosol.
02:54
Protein Kinases and Phosphatases
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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...
08:05
Assaying Protein Kinase Activity with Radiolabeled ATP
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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.
11:13
Identification of Kinase-substrate Pairs Using High Throughput Screening
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Cited by 1 •
2015
Protein phosphorylation is a central feature of how cells interpret and respond to information in their extracellular milieu. Here, we present a high throughput screening protocol using kinases purified from mammalian cells to rapidly identify kinases that phosphorylate a substrate(s) of interest.
FAQs
Receptor activation stimulates phosphoinositide 3-kinases at the plasma membrane, where they generate phosphatidylinositol-3,4,5-trisphosphate. This lipid serves as a membrane-associated signal that recruits AKT and other downstream effectors. Their subsequent activation converts an extracellular cue into intracellular programs controlling cellular survival, metabolism, growth, and immune behavior.
Phosphatidylinositol-3,4,5-trisphosphate provides a localized signaling platform at the plasma membrane. By recruiting AKT and additional downstream effectors, it helps organize the intracellular response close to the activated receptor. This spatial step matters because receptor stimulation must be translated into coordinated cellular actions rather than remaining an unconnected extracellular signal.
Pathogens may exploit or disrupt this signaling pathway to change host-cell behavior and influence immune defenses. Altering pathway activity can affect processes such as leukocyte activation, migration, phagocytosis, or cytokine production. Examining these changes helps connect microbial signals with altered host responses and clarifies how infection can reshape cellular communication.
Studies can assess several distinct outcomes, including leukocyte activation, movement, phagocytosis, and cytokine production. These readouts reflect different aspects of immune-cell behavior, so together they provide a broader view of how signaling influences host responses. They are especially relevant when comparing responses to extracellular cues or microbial signals during infection.
The pathway is particularly informative when researchers examine how immune cells respond to microbial signals or how pathogens modify host defenses. Its relevance extends from early cellular responses, such as leukocyte migration and phagocytosis, to cytokine production and other immune outcomes. This makes it useful for linking molecular signaling events with infection-related cellular behavior.
Understanding pathway regulation may help identify interventions that adjust infection-related inflammation without broadly suppressing immunity. The goal is to connect specific signaling changes with outcomes such as cytokine production, leukocyte activation, or phagocytosis. Such analysis can guide therapeutic strategies that modulate harmful or excessive responses while preserving more general host-defense functions.