دورية أكاديمية
Cdc14 phosphatases preferentially dephosphorylate a subset of cyclin-dependent kinase (Cdk) sites containing phosphoserine.
| العنوان: | Cdc14 phosphatases preferentially dephosphorylate a subset of cyclin-dependent kinase (Cdk) sites containing phosphoserine. |
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| المؤلفون: | Bremmer SC; Department of Biochemistry, Purdue Center for Cancer Research, Purdue University, West Lafayette, Indiana 47907, USA., Hall H, Martinez JS, Eissler CL, Hinrichsen TH, Rossie S, Parker LL, Hall MC, Charbonneau H |
| المصدر: | The Journal of biological chemistry [J Biol Chem] 2012 Jan 13; Vol. 287 (3), pp. 1662-9. Date of Electronic Publication: 2011 Nov 23. |
| نوع المنشور: | Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology |
| مواضيع طبية MeSH: | Cyclin-Dependent Kinases/*metabolism , Dual-Specificity Phosphatases/*metabolism , Phosphoprotein Phosphatases/*metabolism , Phosphoric Monoester Hydrolases/*metabolism , Schizosaccharomyces/*enzymology , Schizosaccharomyces pombe Proteins/*metabolism, Amino Acid Substitution ; Cyclin-Dependent Kinases/chemistry ; Cyclin-Dependent Kinases/genetics ; Dual-Specificity Phosphatases/chemistry ; Dual-Specificity Phosphatases/genetics ; Humans ; Mutation, Missense ; Phosphoprotein Phosphatases/chemistry ; Phosphoprotein Phosphatases/genetics ; Phosphoric Monoester Hydrolases/chemistry ; Phosphoric Monoester Hydrolases/genetics ; Phosphorylation/physiology ; Phosphoserine/chemistry ; Phosphoserine/metabolism ; Protein Tyrosine Phosphatases ; Schizosaccharomyces/genetics ; Schizosaccharomyces pombe Proteins/chemistry ; Schizosaccharomyces pombe Proteins/genetics ; Substrate Specificity/physiology |
| مستخلص: | Mitotic cell division is controlled by cyclin-dependent kinases (Cdks), which phosphorylate hundreds of protein substrates responsible for executing the division program. Cdk inactivation and reversal of Cdk-catalyzed phosphorylation are universal requirements for completing and exiting mitosis and resetting the cell cycle machinery. Mechanisms that define the timing and order of Cdk substrate dephosphorylation remain poorly understood. Cdc14 phosphatases have been implicated in Cdk inactivation and are thought to be generally specific for Cdk-type phosphorylation sites. We show that budding yeast Cdc14 possesses a strong and unusual preference for phosphoserine over phosphothreonine at Pro-directed sites in vitro. Using serine to threonine substitutions in the Cdk consensus sites of the Cdc14 substrate Acm1, we demonstrate that phosphoserine specificity exists in vivo. Furthermore, it appears to be a conserved property of all Cdc14 family phosphatases. An invariant active site residue was identified that sterically restricts phosphothreonine binding and is largely responsible for phosphoserine selectivity. Optimal Cdc14 substrates also possessed a basic residue at the +3 position relative to the phosphoserine, whereas substrates lacking this basic residue were not effectively hydrolyzed. The intrinsic selectivity of Cdc14 may help establish the order of Cdk substrate dephosphorylation during mitotic exit and contribute to roles in other cellular processes. |
| التعليقات: | Comment in: J Biol Chem. 2012 Jan 13;287(3):1670. (PMID: 22247558) |
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| معلومات مُعتمدة: | R01 CA059935 United States CA NCI NIH HHS; CA59935 United States CA NCI NIH HHS |
| المشرفين على المادة: | 0 (Schizosaccharomyces pombe Proteins) 17885-08-4 (Phosphoserine) EC 2.7.11.22 (Cyclin-Dependent Kinases) EC 3.1.3.16 (CDC14 protein, S pombe) EC 3.1.3.16 (Phosphoprotein Phosphatases) EC 3.1.3.2 (Phosphoric Monoester Hydrolases) EC 3.1.3.48 (CDC14A protein, human) EC 3.1.3.48 (CDC14B protein, human) EC 3.1.3.48 (Dual-Specificity Phosphatases) EC 3.1.3.48 (Protein Tyrosine Phosphatases) |
| تواريخ الأحداث: | Date Created: 20111126 Date Completed: 20120305 Latest Revision: 20211021 |
| رمز التحديث: | 20221213 |
| مُعرف محوري في PubMed: | PMC3265848 |
| DOI: | 10.1074/jbc.M111.281105 |
| PMID: | 22117071 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1083-351X |
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| DOI: | 10.1074/jbc.M111.281105 |