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Whi2
Whi2 or Whiskey 2 is a 55 kDa globular, cytoplasmatic scaffold protein in Saccharomyces cerevisiae, which plays an essential role in stress response pathways, apparently by passing input signals about nutrient availability on to stress responsive elements and autophagy/mitophagy mechanisms. It is encoded by a 1.46 kbp gene located on chromosome 15. Functional mechanism Upon complexing with plasma membrane associated phosphatase Psr1, Whi2 induces general stress response by dephosphorylating general stress response transcription factor Msn2. Whi2 is essential for Msn2 activity, moreover activation by Whi2 is dominant and independent of the PKA and TOR activation pathways. Additionally, experiments are suggesting Whi2 for playing a role in Ras2 Ras2 is a ''Saccharomyces cerevisiae'' guanine nucleotide-binding protein (encoded by the RAS2 gene) which becomes activated by binding GTP when glucose is present in the environment. It affects growth regulation and starvation response. M ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ras2
Ras2 is a ''Saccharomyces cerevisiae'' guanine nucleotide-binding protein (encoded by the RAS2 gene) which becomes activated by binding GTP when glucose is present in the environment. It affects growth regulation and starvation response. Modifications Ras2 becomes post-translationally modified in two ways, both being necessary for its activity: Upon activation, palmitoylation at its C terminus takes place and causes attachment from the cytoplasm to the plasma membrane. Farnesylation allows for efficient interaction with the downstream adenylate cyclase Cyr1p. In wild-type yeast deactivated Ras2 is transported to and degraded in the vacuole, a process for which Whi2 is essential. Disturbing this process leads to Ras2 accumulation at the mitochondrial membrane, a behavior that was not observed before. Ras2-cAMP-PKA pathway When activating the adenylate cyclase, Ras2 indirectly raises the cellular cAMP levels, thereby activating the PKA, by which in turn it is downregulated. Dow ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Globular Protein
In biochemistry, globular proteins or spheroproteins are spherical ("globe-like") proteins and are one of the common protein types (the others being fibrous, disordered and membrane proteins). Globular proteins are somewhat water-soluble (forming colloids in water), unlike the fibrous or membrane proteins. There are multiple fold classes of globular proteins, since there are many different architectures that can fold into a roughly spherical shape. The term globin can refer more specifically to proteins including the globin fold. Globular structure and solubility The term globular protein is quite old (dating probably from the 19th century) and is now somewhat archaic given the hundreds of thousands of proteins and more elegant and descriptive structural motif vocabulary. The globular nature of these proteins can be determined without the means of modern techniques, but only by using ultracentrifuges or dynamic light scattering techniques. The spherical structure is induc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Scaffold Protein
In biology, scaffold proteins are crucial regulators of many key signalling pathways. Although scaffolds are not strictly defined in function, they are known to interact and/or bind with multiple members of a signalling pathway, tethering them into complexes. In such pathways, they regulate signal transduction and help localize pathway components (organized in complexes) to specific areas of the cell such as the plasma membrane, the cytoplasm, the nucleus, the Golgi, endosomes, and the mitochondria. History The first signaling scaffold protein discovered was the Ste5 protein from the yeast ''Saccharomyces cerevisiae''. Three distinct domains of Ste5 were shown to associate with the protein kinases Ste11, Ste7, and Fus3 to form a multikinase complex. Function Scaffold proteins act in at least four ways: tethering signaling components, localizing these components to specific areas of the cell, regulating signal transduction by coordinating positive and negative feedback s ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Saccharomyces Cerevisiae
''Saccharomyces cerevisiae'' () (brewer's yeast or baker's yeast) is a species of yeast (single-celled fungus microorganisms). The species has been instrumental in winemaking, baking, and brewing since ancient times. It is believed to have been originally isolated from the skin of grapes. It is one of the most intensively studied eukaryotic model organisms in molecular biology, molecular and cell biology, much like ''Escherichia coli'' as the model bacteria, bacterium. It is the microorganism behind the most common type of fermentation (biochemistry), fermentation. ''S. cerevisiae'' cells are round to ovoid, 5–10 micrometre, μm in diameter. It reproduces by budding. Many proteins important in human biology were first discovered by studying their Homology (biology), homologs in yeast; these proteins include cell cycle proteins, signaling proteins, and protein-processing enzymes. ''S. cerevisiae'' is currently the only yeast cell known to have Berkeley body, Berkeley bo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Msn2
MSN (meaning Microsoft Network) is a web portal and related collection of Internet services and apps for Windows and mobile devices, provided by Microsoft and launched on August 24, 1995, alongside the release of Windows 95. The Microsoft Network was initially a subscription-based dial-up online service that later became an Internet service provider named MSN Dial-up. At the same time, the company launched a new web portal named Microsoft Internet Start and set it as the first default home page of Internet Explorer, its web browser. In 1998, Microsoft renamed and moved this web portal to the domain name www.msn.com, where it has remained. In addition to its original MSN Dial-up service, Microsoft has used the 'MSN' brand name for a wide variety of products and services over the years, notably Hotmail (later Outlook.com), Messenger (which was once synonymous with 'MSN' in Internet slang and has now been replaced by Skype), and its web search engine, which is now Bing, and se ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Kinase A
In cell biology, protein kinase A (PKA) is a family of enzymes whose activity is dependent on cellular levels of cyclic AMP (cAMP). PKA is also known as cAMP-dependent protein kinase (). PKA has several functions in the cell, including regulation of glycogen, sugar, and lipid metabolism. It should not be confused with 5'-AMP-activated protein kinase (AMP-activated protein kinase). History Protein kinase A, more precisely known as adenosine 3',5'-monophosphate (cyclic AMP)-dependent protein kinase, abbreviated to PKA, was discovered by chemists Edmond H. Fischer and Edwin G. Krebs in 1968. They won the Nobel Prize in Physiology or Medicine in 1992 for their work on phosphorylation and dephosphorylation and how it relates to PKA activity. PKA is one of the most widely researched protein kinases, in part because of its uniqueness; out of 540 different protein kinase genes that make up the human kinome, only one other protein kinase, casein kinase 2, is known to exist in a physio ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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