Proteomics

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4-Oxo-2-nonenal Adductions in Cells

ABSTRACT: 4-Oxo-2-nonenal (ONE) derived from lipid peroxidation modifies nucleophiles and transduces redox signaling by its reactions with proteins. However, the molecular interactions between ONE and complex proteomes and their dynamics in situ remain largely unknown. Here we de-scribe a quantitative chemoproteomic analysis of protein adduction by ONE in cells, in which the cellular target profile of ONE is mimicked by its alkynyl surrogate. The analysis reveals four types of ONE-derived modifications in cells, including ketoamide and Schiff-base adducts to lysine, Michael adducts to cysteine, and a novel pyrrole adducts to cysteine. ONE-derived adducts co-localize and crosstalk with many histone marks and redox sensitive sites. All four types of modifications derived from ONE can be reversed site-specifically in cells. In summary, our study provides much-needed mechanistic insights into the cellular signaling and potential toxicities associated with this important lipid derived electrophile.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell

SUBMITTER: Jing Yang  

LAB HEAD: Yang Jing

PROVIDER: PXD007149 | Pride | 2017-08-25

REPOSITORIES: Pride

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JY_RKO_aONE_PC0h_20150419_BR1_T1.mzML Mzml
JY_RKO_aONE_PC0h_20150419_BR1_T1.pride.mgf.gz Mgf
JY_RKO_aONE_PC0h_20150419_BR1_T1.raw Raw
JY_RKO_aONE_PC0h_20150419_BR1_T1_MG.mzid.gz Mzid
JY_RKO_aONE_PC0h_20150419_BR1_T1_MG.pride.mztab.gz Mztab
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Publications

Chemoproteomics Reveals Chemical Diversity and Dynamics of 4-Oxo-2-nonenal Modifications in Cells.

Sun Rui R   Fu Ling L   Liu Keke K   Tian Caiping C   Yang Yong Y   Tallman Keri A KA   Porter Ned A NA   Liebler Daniel C DC   Yang Jing J  

Molecular & cellular proteomics : MCP 20170816 10

4-Oxo-2-nonenal (ONE) derived from lipid peroxidation modifies nucleophiles and transduces redox signaling by its reactions with proteins. However, the molecular interactions between ONE and complex proteomes and their dynamics <i>in situ</i> remain largely unknown. Here we describe a quantitative chemoproteomic analysis of protein adduction by ONE in cells, in which the cellular target profile of ONE is mimicked by its alkynyl surrogate. The analyses reveal four types of ONE-derived modificatio  ...[more]

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