دورية أكاديمية
Measuring Activity and Specificity of Protein Phosphatases.
| العنوان: | Measuring Activity and Specificity of Protein Phosphatases. |
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| المؤلفون: | Powers BL; Department of Biochemistry and Center for Cancer Research, Purdue University, West Lafayette, IN, 47907, USA., Melesse M, Eissler CL, Charbonneau H, Hall MC |
| المصدر: | Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2016; Vol. 1342, pp. 221-35. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Humana Press Country of Publication: United States NLM ID: 9214969 Publication Model: Print Cited Medium: Internet ISSN: 1940-6029 (Electronic) Linking ISSN: 10643745 NLM ISO Abbreviation: Methods Mol Biol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Totowa, NJ : Humana Press Original Publication: Clifton, N.J. : Humana Press, |
| مواضيع طبية MeSH: | Enzyme Assays/*methods , Phosphoprotein Phosphatases/*metabolism, Chromatography, Liquid ; Mass Spectrometry ; Phosphopeptides/chemistry ; Phosphopeptides/metabolism ; Phosphorylation ; Substrate Specificity |
| مستخلص: | Reversible protein phosphorylation plays essential roles in coordinating cell division and many other biological processes. Cell cycle regulation by opposing kinase and protein phosphatase activities is often complex and major challenges exist in identifying the direct substrates of these enzymes and the specific sites at which they act. While cell cycle kinases are known to exhibit strict substrate specificities important for coordinating the complex events of cell division, phosphatases have only recently been recognized to exert similarly precise regulatory control over cell cycle events through timely dephosphorylation of specific substrates. The molecular determinants for substrate recognition by many phosphatases that function in cell division are still poorly delineated. To understand phosphatase specificity, it is critical to employ methods that monitor the dephosphorylation of individual phosphorylation sites on physiologically relevant substrates. Here, using the cell cycle phosphatase Cdc14 as an example, we describe two methods for studying phosphatase specificity, one using synthetic phosphopeptide substrates and the other using intact phosphoprotein substrates. These methods are useful for targeted characterization of small substrate sets and are also adaptable to large-scale applications for global specificity studies. |
| المشرفين على المادة: | 0 (Phosphopeptides) EC 3.1.3.16 (Phosphoprotein Phosphatases) |
| تواريخ الأحداث: | Date Created: 20150810 Date Completed: 20160506 Latest Revision: 20150810 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1007/978-1-4939-2957-3_13 |
| PMID: | 26254927 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1940-6029 |
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| DOI: | 10.1007/978-1-4939-2957-3_13 |