Receptor Tyrosine Kinase
Receptor Tyrosine Kinase - Related Videos
01:26
Receptor Tyrosine Kinases
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2025
Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
10:49
Pre-clinical Evaluation of Tyrosine Kinase Inhibitors for Treatment of Acute Leukemia
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Cited by 6 •
2013
Receptor tyrosine kinases are ectopically expressed in many cancers and have been identified as therapeutic targets in acute leukemia. This manuscript describes an efficient strategy for pre-clinical evaluation of tyrosine kinase inhibitors for the treatment of acute leukemia.
01:26
Treatment for Pulmonary Arterial Hypertension: Receptor Tyrosine Kinase Inhibitors and Calcium Channel Blockers
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2024
Receptor tyrosine kinase inhibitors (TKIs) and calcium channel blockers (CCBs) are two critical categories of drugs employed in the treatment of pulmonary artery hypertension (PAH). PAH is a disease that causes high blood pressure in the pulmonary arteries, resulting in chest pain, fatigue, and shortness of breath. TKIs, such as imatinib (Gleevec), are particularly effective in tackling the growth and mitogenic factors that become upregulated in PAH patients. These factors contribute to the...
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...
07:42
Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays
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Cited by 1 •
2018
Here, we present a protocol for antibody arrays to identify alterations in signaling pathways in various cellular models. These changes, caused by drugs/hypoxia/ultra-violet light/radiation, or by overexpression/downregulation/knockouts, are important for various disease models and can indicate whether a therapy will be effective or can identify mechanisms of drugs resistance.
FAQs
Ligand binding changes the receptor’s organization by promoting dimerization, which brings the intracellular kinase domains into proximity. The domains then phosphorylate tyrosine residues on one another. This phosphorylation is not merely a chemical modification; it creates binding locations for signaling proteins, allowing an extracellular event to be translated into coordinated intracellular instructions.
Phosphorylated tyrosines function as docking sites that organize downstream signaling proteins at the receptor. Their placement helps connect receptor activation with pathways including RAS-MAPK and PI3K-AKT. Because these pathways influence gene expression and cellular behavior, the receptor can convert a localized surface interaction into broader changes in growth, survival, differentiation, or metabolism.
The involvement of both RAS-MAPK and PI3K-AKT shows that receptor activation can connect an extracellular signal with more than one intracellular signaling route. These pathways provide links to changes in gene expression and cellular behavior rather than producing a single isolated response. This helps explain how RTKs influence several biological processes, including growth, survival, differentiation, and metabolism.
RTKs are important in developmental biology because their signaling can regulate differentiation, growth, survival, and metabolism. Through ligand-triggered receptor activation and downstream pathway engagement, extracellular cues can influence cellular behavior during development. Studying these receptors therefore helps connect cell-surface communication with the coordinated changes required for developmental processes.
Abnormal activation of RTKs is relevant to cancer biology because these receptors normally regulate growth and survival, along with other cellular behaviors. If their signaling becomes dysregulated, the connection between extracellular cues and intracellular instructions may be altered. RTK research therefore provides a framework for examining how signaling abnormalities relate to cancer-associated cellular behavior.
RTKs are studied in diagnostic research because their activation state and signaling relationships connect extracellular signals with measurable cellular behavior. Their importance in growth, survival, differentiation, and metabolism also makes abnormal signaling biologically significant. For this reason, RTKs have become targets for kinase-inhibitor therapies, while diagnostic research examines their relevance to disease-associated signaling.