Jun Amino Terminal Kinases
Jun Amino Terminal Kinases - Related Videos
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...
01:44
Termination of Translation
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2020
The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
04:04
Radiolabeled Amino Acid Uptake Assay to Quantify Cellular Uptake of Amino Acids
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2025
This video demonstrates an in vitro technique for estimating amino acid uptake by bone marrow-derived stromal cells. Na+-dependent amino acid transporters mediate the uptake of radiolabeled amino acids inside the cells, and the cellular uptake is estimated by measuring the radioactivity.
06:09
Assaying the Kinase Activity of LRRK2 in vitro
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Cited by 3 •
2012
Leucine Rich Repeat Kinase 2 is a large multidomain kinase, mutations in which are the most common genetic cause of Parkinson's disease. Analysis of the kinase activity of this protein has proven to be a crucial tool in understanding the biology and dysfunction of this protein. In this paper, in vitro assaying of the kinase activity of LRRK2 and a selection of its mutants is described, providing an experimental system to examine phosphorylation of putative substrates and potential dysfunction...
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.
FAQs
Signal transmission proceeds through a phosphorylation cascade in which upstream MAP kinase kinases activate JNKs. Once activated, these kinases phosphorylate transcription factors such as c-Jun. That modification changes transcriptional activity, allowing a signal originating from environmental or physiological stress to influence cellular programs rather than remaining a local molecular event.
JNK activity responds to several forms of cellular challenge, including oxidative stress, cytokines, and other environmental or physiological signals. This range allows the pathway to connect external conditions with intracellular gene regulation. The particular signal matters because JNK signaling can influence different biological responses, including inflammation, differentiation, proliferation, or apoptosis.
The consequences of JNK signaling depend partly on whether activation is limited or persistent. Regulated activation helps cells adjust gene expression during changing conditions, whereas excessive or prolonged activity can contribute to tissue injury and disease. This distinction makes signaling intensity and persistence important considerations when interpreting JNK-related cellular responses.
JNKs provide a mechanistic link between stress-related signals and transcriptional control. By phosphorylating c-Jun and other transcription factors, they can alter expression of genes associated with major cellular decisions. Studying this link helps biology researchers analyze how signal transduction becomes changes in cell behavior, rather than examining gene expression as an isolated endpoint.
JNK signaling is relevant across cancer biology, neurodegeneration, immune responses, and the study of tissue injury. Its importance in these areas follows from its ability to regulate gene-expression programs connected with proliferation, inflammation, differentiation, and apoptosis. Research may therefore examine the pathway both as a source of disease-related effects and as a possible therapeutic target.
Because abnormal or persistent JNK activation can be associated with tissue injury and disease, researchers investigate the pathway as a potential point for targeted intervention. Such work connects molecular signaling studies with therapeutic research in conditions involving cancer, immune responses, neurodegeneration, or other stress-related damage. The goal is to understand when modifying this pathway could be beneficial.