Yingming Zhao, PhD

  • Professor of Ben May Department of Cancer Research
  • Research and Scholarly Interests: Proteomics, epigenetics, protein modifications, cancer, metabolism, Warburg effect
  • Websites: Research Network Profile
  • Contact: yzhao4@uchicago.edu

Post-translational modifications (PTMs) represent a major vehicle to diversify a cellular proteome, the inventory of all protein species in an organism. PTMs have critical roles in all the major cellular pathways and diseases. A protein can be potentially modified by more than 300 types of post-translational modifications, which are catalyzed by enzymes encoded by more than 5% of the genome in higher eukaryotes. A combination of a dozen PTM sites in a substrate protein could lead to more than a million possible protein structures with potentially different functions. Given the high abundance and diversities of PTMs, they are likely the most complex regulatory mechanisms in cells. Despite their critical roles in cells, little is known about their biology, except several most extensively studied PTMs. Functional characterizations of PTMs at the molecular level have been slow, largely due to a lack of suitable information infrastructure and technology infrastructure.

The Rockefeller University
New York city
PhD
1997

Lysine benzoylation is a histone mark regulated by SIRT2.
Huang H, Zhang D, Wang Y, Perez-Neut M, Han Z, Zheng YG, Hao Q, Zhao Y. Lysine benzoylation is a histone mark regulated by SIRT2. Nat Commun. 2018 08 28; 9(1):3374.
PMID: 30154464

p300-Mediated Lysine 2-Hydroxyisobutyrylation Regulates Glycolysis.
Huang H, Tang S, Ji M, Tang Z, Shimada M, Liu X, Qi S, Locasale JW, Roeder RG, Zhao Y, Li X. p300-Mediated Lysine 2-Hydroxyisobutyrylation Regulates Glycolysis. Mol Cell. 2018 06 07; 70(5):984.
PMID: 29883613

Intracellular Crotonyl-CoA Stimulates Transcription through p300-Catalyzed Histone Crotonylation.
Sabari BR, Tang Z, Huang H, Yong-Gonzalez V, Molina H, Kong HE, Dai L, Shimada M, Cross JR, Zhao Y, Roeder RG, Allis CD. Intracellular Crotonyl-CoA Stimulates Transcription through p300-Catalyzed Histone Crotonylation. Mol Cell. 2018 02 01; 69(3):533.
PMID: 29395068

Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation pathway.
Huang H, Luo Z, Qi S, Huang J, Xu P, Wang X, Gao L, Li F, Wang J, Zhao W, Gu W, Chen Z, Dai L, Dai J, Zhao Y. Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation pathway. Cell Res. 2018 01; 28(1):111-125.
PMID: 29192674

ACSF3 and Mal(onate)-Adapted Mitochondria.
Lombard DB, Zhao Y. ACSF3 and Mal(onate)-Adapted Mitochondria. Cell Chem Biol. 2017 Jun 22; 24(6):649-650.
PMID: 28644952

Metabolic regulation of gene expression through histone acylations.
Sabari BR, Zhang D, Allis CD, Zhao Y. Metabolic regulation of gene expression through histone acylations. Nat Rev Mol Cell Biol. 2017 02; 18(2):90-101.
PMID: 27924077

Metabolic Regulation of Gene Expression by Histone Lysine ß-Hydroxybutyrylation.
Xie Z, Zhang D, Chung D, Tang Z, Huang H, Dai L, Qi S, Li J, Colak G, Chen Y, Xia C, Peng C, Ruan H, Kirkey M, Wang D, Jensen LM, Kwon OK, Lee S, Pletcher SD, Tan M, Lombard DB, White KP, Zhao H, Li J, Roeder RG, Yang X, Zhao Y. Metabolic Regulation of Gene Expression by Histone Lysine ß-Hydroxybutyrylation. Mol Cell. 2016 04 21; 62(2):194-206.
PMID: 27105115

Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation.
Colak G, Pougovkina O, Dai L, Tan M, Te Brinke H, Huang H, Cheng Z, Park J, Wan X, Liu X, Yue WW, Wanders RJ, Locasale JW, Lombard DB, de Boer VC, Zhao Y. Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation. Mol Cell Proteomics. 2015 Nov; 14(11):3056-71.
PMID: 26320211

SnapShot: histone modifications.
Huang H, Sabari BR, Garcia BA, Allis CD, Zhao Y. SnapShot: histone modifications. Cell. 2014 Oct 09; 159(2):458-458.e1.
PMID: 25303536

Lysine glutarylation is a protein posttranslational modification regulated by SIRT5.
Tan M, Peng C, Anderson KA, Chhoy P, Xie Z, Dai L, Park J, Chen Y, Huang H, Zhang Y, Ro J, Wagner GR, Green MF, Madsen AS, Schmiesing J, Peterson BS, Xu G, Ilkayeva OR, Muehlbauer MJ, Braulke T, Mühlhausen C, Backos DS, Olsen CA, McGuire PJ, Pletcher SD, Lombard DB, Hirschey MD, Zhao Y. Lysine glutarylation is a protein posttranslational modification regulated by SIRT5. Cell Metab. 2014 Apr 01; 19(4):605-17.
PMID: 24703693

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