Yeast Kinase
Yeast Kinase - 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...
08:30
Yeast Maintenance
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2023
Research performed in the yeast Saccharomyces cerevisiae has significantly improved our understanding of important cellular phenomona such as regulation of the cell cycle, aging, and cell death. The many benefits of working with S. cerevisiae include the facts that they are inexpensive to grow in the lab and that many ready-to-use strains are now commercially available. Nevertheless, proper maintenance of this organism is critical for successful experiments. This video will provide an overview...
07:48
Yeast Reproduction
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2023
Saccharomyces cerevisiae is a species of yeast that is an extremely valuable model organism. Importantly, S. cerevisiae is a unicellular eukaryote that undergoes many of the same biological processes as humans. This video provides an introduction to the yeast cell cycle, and explains how S. cerevisiae reproduces both asexually and sexually Yeast reproduce asexually through a process known as budding. In contrast, yeast sometimes participate in sexual reproduction, which is important because...
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...
05:20
Yeast Two-Hybrid Assay to Determine Protein Self-Association in Yeast Cells
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2025
This video demonstrates the yeast two-hybrid assay to detect specific protein self-interactions. In this assay, the protein of interest is tagged to two domains of a transcription factor that encodes the β-galactosidase enzyme. When the two proteins interact, this causes transcription and translation to form the enzyme, which is then detected using a biochemical assay.
FAQs
A kinase does not phosphorylate every molecule indiscriminately. It recognizes particular substrates and transfers phosphate in a way that can change a target’s activity, stability, cellular location, or molecular interactions. Consequently, identifying the relevant substrate helps researchers connect one phosphorylation event with a broader cellular outcome, such as altered growth, metabolism, stress response, or gene expression.
ATP supplies the phosphate group used in the kinase reaction, linking cellular energy status to regulatory signaling. The enzyme uses ATP as a donor while acting on a specific target, so changes in kinase activity can influence multiple downstream processes. Studying this dependence helps clarify how phosphorylation networks regulate cell division, growth, metabolism, and stress responses.
The distinction is based on the type of molecular target associated with phosphorylation. Protein kinases act on protein substrates, whereas lipid kinases are identified by their relationship to lipid targets. Separating these classes helps researchers organize signaling mechanisms and determine whether a cellular response reflects altered protein regulation, lipid-related regulation, or connections between these forms of control.
Genetic analysis can link a kinase to a cellular process by examining how changes affecting the kinase alter cell behavior or signaling outcomes. When the resulting phenotype relates to growth, division, metabolism, stress responses, or gene expression, researchers gain evidence about the pathway in which the kinase functions. This approach is especially valuable because yeast supports tractable genetic investigation.
Biochemical assays examine the kinase reaction directly, including phosphate transfer from ATP to an appropriate molecular target. They can help establish whether a kinase is active, identify substrate relationships, and connect enzymatic activity with a proposed signaling mechanism. These measurements complement genetic evidence by testing the molecular event underlying an observed cellular effect.
Kinase-inhibitor studies are useful when researchers need to test whether a signaling outcome depends on kinase activity. Comparing cellular or molecular responses in the presence and absence of inhibition can help distinguish kinase-dependent effects from unrelated changes. Together with genetic and biochemical approaches, inhibitor results strengthen interpretations of phosphorylation networks and their roles in cell regulation.
Yeast kinases provide tractable systems for investigating signaling pathways that are conserved across biology. Researchers can connect phosphorylation mechanisms controlling growth, division, metabolism, stress responses, or gene expression in yeast with related processes in disease biology. Findings from these models may also inform the study of therapeutic strategies, particularly when genetic, biochemical, and inhibitor-based evidence converge.