Phosphorylation Cascade

A phosphorylation cascade is a sequential cell-signaling process in which one protein kinase activates another, allowing extracellular information to produce coordinated intracellular responses. Typically, receptor stimulation initiates kinase activity; each kinase transfers a phosphate group from ATP to specific target proteins, while protein phosphatases remove these groups to regulate signal duration and intensity. In pharmacology, phosphorylation cascades help explain how hormones, growth factors, and medicines alter gene expression, metabolism, proliferation, or cell survival. Mapping these pathways supports the development of kinase inhibitors and other targeted therapies, while also clarifying mechanisms of drug action, resistance, and adverse effects.

Phosphorylation Cascade - Related Videos

Education

JoVE Core - Biology

Phosphorylation

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2019

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins. During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...

Phosphorylation

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2020

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins. During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...

Rab Cascades

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2023

Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.

Research

JoVE EoE - Assay Techniques

Single-Molecule Pull-Down Assay for Protein Phosphorylation Analysis: A High Throughput Technique to Quantify Protein Phosphorylation in Cell Lysate

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2025

This video demonstrates a sensitive quantification technique of protein phosphorylation using a single-molecule pull-down assay. The functionalization of polyethylene glycol-biotin and the use of labeled antibodies increases the detection of phosphorylated tyrosine with specificity.

Oligopeptide Competition Assay for Phosphorylation Site Determination

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Cited by 3 •

2017

Peptide competition assays are widely used in a variety of molecular and immunological experiments. This paper describes a detailed method for an in vitro oligopeptide-competing kinase assay and the associated validation procedures, which may be useful to find specific phosphorylation sites.

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