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Identification of EGLN2 binding partners using AP-MS

ABSTRACT: Protein binding parnters of EGLN2 were identified in response to DMOG treatment.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Laura Herring

LAB HEAD: Qing Zhang

PROVIDER: PXD015787 | Pride | 2019-11-20

REPOSITORIES: Pride

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			Action	DRS
	20160713_PC132-Zhang_APMS_S1-test.msf	Msf
	20160713_PC132-Zhang_APMS_S1-test.msfView	Msf
	20160713_PC132-Zhang_APMS_S1-test.pdResult	Other
	20160713_PC132-Zhang_APMS_S1-test.pdResultView	Other
	20160713_PC132-Zhang_APMS_S1-test.raw	Raw

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Publications

Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer.

Zurlo Giada G Liu Xijuan X Takada Mamoru M Fan Cheng C Simon Jeremy M JM Ptacek Travis S TS Rodriguez Javier J von Kriegsheim Alex A Liu Juan J Locasale Jason W JW Robinson Adam A Zhang Jing J Holler Jessica M JM Kim Baek B Zikánová Marie M Bierau Jörgen J Xie Ling L Chen Xian X Li Mingjie M Perou Charles M CM Zhang Qing Q

Nature communications 20191115 1

Protein hydroxylation affects protein stability, activity, and interactome, therefore contributing to various diseases including cancers. However, the transiency of the hydroxylation reaction hinders the identification of hydroxylase substrates. By developing an enzyme-substrate trapping strategy coupled with TAP-TAG or orthogonal GST- purification followed by mass spectrometry, we identify adenylosuccinate lyase (ADSL) as an EglN2 hydroxylase substrate in triple negative breast cancer (TNBC). A ...[more]

PMID: 31729379

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