Receptor Like Kinases
Receptor Like Kinases - 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...
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...
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...
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.
11:13
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
Recognition at the extracellular region changes the signaling state of the receptor, allowing its intracellular kinase domain to promote phosphorylation of the receptor and downstream signaling proteins. This creates a molecular relay between environmental information and cellular activity. The resulting response can influence growth, differentiation, development, stress reactions, or innate immunity.
Phosphorylation provides the key intracellular step that carries information beyond the membrane. When receptor-like kinase activation promotes phosphorylation of the receptor and associated signaling proteins, the signal can be distributed through a downstream pathway rather than remaining at the cell surface. This helps connect a particular extracellular cue with an appropriate biological response.
The extracellular domain can bind a ligand or recognize a molecular pattern, so the initiating information depends on the cue encountered by the cell. Once signaling begins, phosphorylation of downstream proteins links that recognition event to a response. Consequently, receptor-like kinases can participate in distinct processes, including development, stress responses, growth, and innate immunity.
In plants, receptor-like kinases are especially important for interpreting information from the surrounding environment. Their signaling pathways contribute to developmental regulation, stress responses, and innate immunity, allowing plant cells to coordinate internal activity with external conditions. This makes them relevant to both fundamental biology and questions about how plants respond to challenges.
A basic investigation can follow the pathway from the initiating ligand or molecular pattern to receptor activation, phosphorylation of the receptor, phosphorylation of downstream signaling proteins, and the resulting cellular response. Organizing observations in this sequence helps researchers determine how an extracellular cue is translated into changes in growth, development, stress response, or immunity.
This research can clarify how cells communicate with their environment and how signaling controls major biological processes. In plant studies, it can connect receptor activity with disease resistance, development, and stress responses. Such knowledge also supports efforts to understand receptor pathways that may improve crop performance, while preserving the connection between molecular signaling and whole-plant outcomes.