Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer
The hydroxylase EgIN2 contributes to triple negative breast cancers. Here, using an enzyme-substrate trapping strategy, the authors identify ASDL as a bona fide substrate of EgIN2 promoting aggressive properties of TNBC via the activation of cMYC signaling.
| Main Authors: | , , , , , , , , , , , , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Publishing Group
2019-11-01
|
| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-019-13168-4 |
| id |
doaj-4f3b6b5738bf4496a2ce34dde8289124 |
|---|---|
| record_format |
Article |
| spelling |
doaj-4f3b6b5738bf4496a2ce34dde82891242021-05-11T12:18:32ZengNature Publishing GroupNature Communications2041-17232019-11-0110111510.1038/s41467-019-13168-4Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancerGiada Zurlo0Xijuan Liu1Mamoru Takada2Cheng Fan3Jeremy M. Simon4Travis S. Ptacek5Javier Rodriguez6Alex von Kriegsheim7Juan Liu8Jason W. Locasale9Adam Robinson10Jing Zhang11Jessica M. Holler12Baek Kim13Marie Zikánová14Jörgen Bierau15Ling Xie16Xian Chen17Mingjie Li18Charles M. Perou19Qing Zhang20Lineberger Comprehensive Cancer Center, University of North Carolina School of MedicineLineberger Comprehensive Cancer Center, University of North Carolina School of MedicineLineberger Comprehensive Cancer Center, University of North Carolina School of MedicineLineberger Comprehensive Cancer Center, University of North Carolina School of MedicineLineberger Comprehensive Cancer Center, University of North Carolina School of MedicineLineberger Comprehensive Cancer Center, University of North Carolina School of MedicineCancer Research UK Edinburgh Centre, IGMM, University of EdinburghCancer Research UK Edinburgh Centre, IGMM, University of EdinburghDepartment of Pharmacology and Cancer Biology, Duke University School of MedicineDepartment of Pharmacology and Cancer Biology, Duke University School of MedicineLineberger Comprehensive Cancer Center, University of North Carolina School of MedicineLineberger Comprehensive Cancer Center, University of North Carolina School of MedicineDepartment of Pediatrics, School of Medicine, Emory UniversityDepartment of Pediatrics, School of Medicine, Emory UniversityResearch Unit for Rare Diseases, Department of Pediatrics and Adolescent Medicine, First Faculty of Medicine, Charles University and General University Hospital in PragueDepartment of Clinical Genetics, Maastricht University Medical CentreDepartment of Biochemistry and Biophysics, University of North CarolinaDepartment of Biochemistry and Biophysics, University of North CarolinaLineberger Comprehensive Cancer Center, University of North Carolina School of MedicineLineberger Comprehensive Cancer Center, University of North Carolina School of MedicineLineberger Comprehensive Cancer Center, University of North Carolina School of MedicineThe hydroxylase EgIN2 contributes to triple negative breast cancers. Here, using an enzyme-substrate trapping strategy, the authors identify ASDL as a bona fide substrate of EgIN2 promoting aggressive properties of TNBC via the activation of cMYC signaling.https://doi.org/10.1038/s41467-019-13168-4 |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Giada Zurlo Xijuan Liu Mamoru Takada Cheng Fan Jeremy M. Simon Travis S. Ptacek Javier Rodriguez Alex von Kriegsheim Juan Liu Jason W. Locasale Adam Robinson Jing Zhang Jessica M. Holler Baek Kim Marie Zikánová Jörgen Bierau Ling Xie Xian Chen Mingjie Li Charles M. Perou Qing Zhang |
| spellingShingle |
Giada Zurlo Xijuan Liu Mamoru Takada Cheng Fan Jeremy M. Simon Travis S. Ptacek Javier Rodriguez Alex von Kriegsheim Juan Liu Jason W. Locasale Adam Robinson Jing Zhang Jessica M. Holler Baek Kim Marie Zikánová Jörgen Bierau Ling Xie Xian Chen Mingjie Li Charles M. Perou Qing Zhang Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer Nature Communications |
| author_facet |
Giada Zurlo Xijuan Liu Mamoru Takada Cheng Fan Jeremy M. Simon Travis S. Ptacek Javier Rodriguez Alex von Kriegsheim Juan Liu Jason W. Locasale Adam Robinson Jing Zhang Jessica M. Holler Baek Kim Marie Zikánová Jörgen Bierau Ling Xie Xian Chen Mingjie Li Charles M. Perou Qing Zhang |
| author_sort |
Giada Zurlo |
| title |
Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer |
| title_short |
Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer |
| title_full |
Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer |
| title_fullStr |
Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer |
| title_full_unstemmed |
Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer |
| title_sort |
prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer |
| publisher |
Nature Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2019-11-01 |
| description |
The hydroxylase EgIN2 contributes to triple negative breast cancers. Here, using an enzyme-substrate trapping strategy, the authors identify ASDL as a bona fide substrate of EgIN2 promoting aggressive properties of TNBC via the activation of cMYC signaling. |
| url |
https://doi.org/10.1038/s41467-019-13168-4 |
| work_keys_str_mv |
AT giadazurlo prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT xijuanliu prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT mamorutakada prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT chengfan prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT jeremymsimon prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT travissptacek prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT javierrodriguez prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT alexvonkriegsheim prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT juanliu prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT jasonwlocasale prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT adamrobinson prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT jingzhang prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT jessicamholler prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT baekkim prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT mariezikanova prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT jorgenbierau prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT lingxie prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT xianchen prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT mingjieli prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT charlesmperou prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer AT qingzhang prolylhydroxylasesubstrateadenylosuccinatelyaseisanoncogenicdriverintriplenegativebreastcancer |
| _version_ |
1721445035883364352 |