دورية أكاديمية
Divergent JNK Phosphorylation of HDAC3 in Triple-Negative Breast Cancer Cells Determines HDAC Inhibitor Binding and Selectivity.
| العنوان: | Divergent JNK Phosphorylation of HDAC3 in Triple-Negative Breast Cancer Cells Determines HDAC Inhibitor Binding and Selectivity. |
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| المؤلفون: | Hanigan TW; Department of Medicinal Chemistry and Pharmacognosy, College of Pharmacy, University of Illinois at Chicago, 833 South Wood Street, Chicago, IL 60612, USA., Aboukhatwa SM; Department of Medicinal Chemistry and Pharmacognosy, College of Pharmacy, University of Illinois at Chicago, 833 South Wood Street, Chicago, IL 60612, USA; Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Tanta University, Tanta, Egypt 31527., Taha TY; Department of Medicinal Chemistry and Pharmacognosy, College of Pharmacy, University of Illinois at Chicago, 833 South Wood Street, Chicago, IL 60612, USA., Frasor J; Department of Physiology and Biophysics, University of Illinois at Chicago, Chicago, IL 60612, USA., Petukhov PA; Department of Medicinal Chemistry and Pharmacognosy, College of Pharmacy, University of Illinois at Chicago, 833 South Wood Street, Chicago, IL 60612, USA. Electronic address: pap4@uic.edu. |
| المصدر: | Cell chemical biology [Cell Chem Biol] 2017 Nov 16; Vol. 24 (11), pp. 1356-1367.e8. Date of Electronic Publication: 2017 Sep 21. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Cell Press Country of Publication: United States NLM ID: 101676030 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2451-9448 (Electronic) Linking ISSN: 24519448 NLM ISO Abbreviation: Cell Chem Biol Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Cambridge, MA : Cell Press, 2016- |
| مواضيع طبية MeSH: | Histone Deacetylases/*metabolism , JNK Mitogen-Activated Protein Kinases/*metabolism, Cell Line, Tumor ; Female ; Histone Deacetylase Inhibitors/chemistry ; Histone Deacetylase Inhibitors/metabolism ; Histone Deacetylases/chemistry ; Histone Deacetylases/genetics ; Humans ; Hydroxamic Acids/chemistry ; Hydroxamic Acids/metabolism ; Isoenzymes/chemistry ; Isoenzymes/genetics ; Isoenzymes/metabolism ; MCF-7 Cells ; Phosphorylation ; Protein Binding ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/chemistry ; Recombinant Proteins/isolation & purification ; Triple Negative Breast Neoplasms/metabolism ; Triple Negative Breast Neoplasms/pathology |
| مستخلص: | Histone deacetylase (HDAC) catalytic activity is regulated by formation of co-regulator complexes and post-translational modification. Whether these mechanisms are transformed in cancer and how this affects the binding and selectivity of HDAC inhibitors (HDACis) is unclear. In this study, we developed a method that identified a 3- to 16-fold increase in HDACi selectivity for HDAC3 in triple-negative breast cancer (TNBC) cells in comparison with luminal subtypes that was not predicted by current practice measurements with recombinant proteins. We found this increase was caused by c-Jun N-terminal kinase (JNK) phosphorylation of HDAC3, was independent of HDAC3 complex composition or subcellular localization, and was associated with a 5-fold increase in HDAC3 enzymatic activity. This study points to HDAC3 and the JNK axes as targets in TNBC, highlights how HDAC phosphorylation affects HDACi binding and selectivity, and outlines a method to identify changes in individual HDAC isoforms catalytic activity, applicable to any disease state. (Copyright © 2017 Elsevier Ltd. All rights reserved.) |
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| معلومات مُعتمدة: | R01 CA131970 United States CA NCI NIH HHS; R21 CA183627 United States CA NCI NIH HHS |
| فهرسة مساهمة: | Keywords: breast cancer; c-Jun N-terminal kinase; co-repressor complex; histone deacetylase; histone deacetylase inhibitor; inhibitor selectivity; phosphorylation; photoreactive probes; target engagement |
| المشرفين على المادة: | 0 (Histone Deacetylase Inhibitors) 0 (Hydroxamic Acids) 0 (Isoenzymes) 0 (Recombinant Proteins) EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases) EC 3.5.1.98 (Histone Deacetylases) EC 3.5.1.98 (histone deacetylase 3) |
| تواريخ الأحداث: | Date Created: 20170926 Date Completed: 20171226 Latest Revision: 20240327 |
| رمز التحديث: | 20240327 |
| مُعرف محوري في PubMed: | PMC5693607 |
| DOI: | 10.1016/j.chembiol.2017.08.015 |
| PMID: | 28943357 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 2451-9448 |
|---|---|
| DOI: | 10.1016/j.chembiol.2017.08.015 |