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Matthew Petroski

Associate Professor
Tumor Initiation and Maintenance Program
Sanford-Burnham Medical Research Institute
United States of America

Biography

Matthew Petroski earned his Ph.D. in Biochemistry and Molecular Biology from the University of California, Irvine, and was a Jane Coffin Childs Fellow and HHMI post-doctoral fellow from 1999-2005 with Ray Deshaies at Caltech. From 2005-2007, Matt was a Research Scientist at Rigel Pharmaceuticals, Inc. in South San Francisco and was recruited to SBP as an Assistant Professor in December 2007.

Research Interest

Our lab focuses on understanding how proteins are modified with ubiquitin and ubiquitin-like proteins. We anticipate that understanding how the ubiquitin system functions and regulates cellular processes will lead to the development of therapeutics that will have broad impact on human health. Alterations in protein function controlled by specific pathways of the ubiquitin system are associated with cancer, inflammation, neurodegenerative diseases, and viral infection. We aim to dissect and study these important pathways using a combination of cell biology, molecular genetics, biochemistry, proteomics, and chemical biology. Our current interests include: mechanisms of ubiquitin chain synthesis and protein modification cellular functions of the ubiquitin-like protein NEDD8 in regulating cullin-RING ubiquitin ligases ubiquitinated protein recognition and delivery to the 26S proteasome

Publications

  • hnRNP K: an HDM2 target and transcriptional coactivator of p53 in response to DNA damage. MOUMEN A, MASTERSON P, O'CONNOR MJ, JACKSON SP Cell 2005 Dec 16;123(6):1065-78

  • Evaluation of a diffusion-driven mechanism for substrate ubiquitination by the SCF-Cdc34 ubiquitin ligase complex. PETROSKI MD, KLEIGER G, DESHAIES RJ Mol Cell 2006 Nov 17;24(4):523-34

  • Substrate modification with lysine 63-linked ubiquitin chains through the UBC13-UEV1A ubiquitin-conjugating enzyme. PETROSKI MD, ZHOU X, DONG G, DANIEL-ISSAKANI S, PAYAN DG, HUANG J J Biol Chem 2007 Oct 12;282(41):29936-45

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