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Eric Strieter

Assistant Professor

The overarching goal of my research program is to understand, on a molecular level, how the small protein ubiquitin controls the dynamics of biochemical pathways to maintain normal cellular function. Ubiquitin (Ub) is covalently tethered to proteins through the action of several enzymes. This process is termed ubiquitination and is one of the most prevalent and complex in all eukaryotic organisms. The complexity of protein ubiquitination arises from the ability of Ub to serve as a substrate for subsequent enzymatic transformations that can lead to polymeric Ub chains, which come in diverse sizes and shapes (e.g., linear or branched). The prevailing view is that the diversity of Ub chain types can fine-tune the dynamics of vital cellular processes such as growth, division, DNA repair, and protein degradation. The question that remains unanswered is how different Ub chains regulate distinct biological processes. To address this key issue, we focus on the enzymes that remove Ub modifications: the deubiquitinases or DUBs. Understanding which Ub chain type is targeted for cleavage by each DUB can reveal the critical link between Ub chain type and cellular pathway. Also unknown is the mechanism by which DUBs catalyze the removal of Ub modifications. Addressing this issue is important, as DUBs are important therapeutic targets, and methods to regulate their activity will emerge from an understanding of DUB molecular mechanisms.

Current Research

  • Developing New Tools for Ubiquitin Biology
  • Understanding the Functions of Ubiquitin C-Terminal Hydrolases
  • Investigating the Mechanisms of Cysteine-Dependent Deubiquitinases
  • Developing Allosteric Inhibitors of Deubiquitinases

Learn more at

Academic Background

  • Assistant Professor of Chemistry, University of Wisconsin-Madison
  • American Cancer Society Postdoctoral Fellow, Harvard Medical School
  • PhD, MIT
  • BS, University of Wisconsin-Madison
Crowe S. O., Pham G. H., Ziegler J. C., Deol K. K., Guenette R. G., Ge Y., Strieter E. R. Subunit-Specific Labeling of Ubiquitin Chains Using Sortase: Insights into the Selectivity of Deubiquitinases. Chembiochem (in press). DOI: 10.1002/cbic.201600276
Pham G. H.†, Rana A. S. J. B.†, Korkmaz E. N.†, Trang V. H., Cui Q., Strieter E. R. Comparison of Native and Non-Native Ubiquitin Oligomers Reveals Analogous Structures and Reactivities. Protein Sci. 2016; 25(2): 456-71. †These authors contributed equally to this work.
Strieter E. R., Andrew T. L. Restricting the ψ Torsion Angle has Stereoelectronic Consequences on a Scissile Bond: An Electronic Structure Analysis. Biochemistry 2015; 54(37): 5748-56.
Shekhawat S. S.†, Pham G. H.†, Prabakaran J., Strieter E. R. Simultaneous Detection of Distinct Ubiquitin Chain Topologies by 19F NMR. ACS Chem. Biol. 2014; 9(10): 2229-36. †These authors contributed equally to this work.
Valkevich E. M., Sanchez N. A., Ge Y., Strieter E. R. Middle-Down Mass Spectrometry Enables Characterization of Branched Ubiquitin Chains. Biochemistry 2014; 53(30): 4979-89.
Trang V. H., Rodgers M. L., Boyle K. J., Hoskins A. A., Strieter E. R. Chemoenzymatic synthesis of bifunctional polyubiquitin substrates for monitoring ubiquitin chain remodeling. Chembiochem 2014; 15(11): 1563-8.
Shrestha K., Ronau J. A., Davies C. W., Guenette R. G., Strieter E. R., Paul L. N., Das C. Insights into the mechanism of deubiquitination by JAMM deubiquitinases from cocrystal structures of the enzyme with the substrate and product. Biochemistry 2014; 53(19): 3199-217.
Hebert A. S., Merrill A. E., Bailey D. J., Still A. J., Westphall M. S., Strieter E. R., Pagliarini D. J., Coon J. J. Neutron-encoded mass signatures for multiplexed proteome quantification. Nat. Methods 2013; 10(4): 332-4.
Trang V. H., Valkevich E. M., Minami S., Chen Y-C., Ge Y., Strieter E. R. Nonenzymatic Polymerization of Ubiquitin: Single-Step Synthesis and Isolation of Discrete Ubiquitin Oligomers. Angew. Chem. Int. Ed. 2012; 51(52): 13085-8.
Valkevich E. M., Guenette R. G., Sanchez N. A., Chen Y-C., Ge Y., Strieter E. R. Forging Isopeptide Bonds Using Thiol-Ene Chemistry: Site-Specific Coupling of Ubiquitin Molecules for Studying the Activity of Isopeptidases. J. Am. Chem. Soc. 2012; 134(16): 6916-9.
Contact Info

Department of Chemistry
710 North Pleasant Street
Amherst, MA 01003-9292