A chemoproteomic portrait of the oncometabolite fumarate View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2019-04

AUTHORS

Rhushikesh A. Kulkarni, Daniel W. Bak, Darmood Wei, Sarah E. Bergholtz, Chloe A. Briney, Jonathan H. Shrimp, Aktan Alpsoy, Abigail L. Thorpe, Arissa E. Bavari, Daniel R. Crooks, Michaella Levy, Laurence Florens, Michael P. Washburn, Norma Frizzell, Emily C. Dykhuizen, Eranthie Weerapana, W. Marston Linehan, Jordan L. Meier

ABSTRACT

Hereditary cancer disorders often provide an important window into novel mechanisms supporting tumor growth. Understanding these mechanisms thus represents a vital goal. Toward this goal, here we report a chemoproteomic map of fumarate, a covalent oncometabolite whose accumulation marks the genetic cancer syndrome hereditary leiomyomatosis and renal cell carcinoma (HLRCC). We applied a fumarate-competitive chemoproteomic probe in concert with LC-MS/MS to discover new cysteines sensitive to fumarate hydratase (FH) mutation in HLRCC cell models. Analysis of this dataset revealed an unexpected influence of local environment and pH on fumarate reactivity, and enabled the characterization of a novel FH-regulated cysteine residue that lies at a key protein-protein interface in the SWI-SNF tumor-suppressor complex. Our studies provide a powerful resource for understanding the covalent imprint of fumarate on the proteome and lay the foundation for future efforts to exploit this distinct aspect of oncometabolism for cancer diagnosis and therapy. More... »

PAGES

391-400

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41589-018-0217-y

DOI

http://dx.doi.org/10.1038/s41589-018-0217-y

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1111907991

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30718813


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