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Research Abstracts Online
January 2008 - March 2009

University of Minnesota Twin Cities
College of Biological Sciences and Medical School
Department of Biochemistry, Molecular Biology, and Biophysics

PI: Kylie J. Walters, Associate Fellow

Studying the Ubiquitin Proteasome Pathway by Nuclear Magnetic Resonance Spectroscopy

These researchers study how the ubiquitin-proteasome pathway targets protein substrates for degradation. Central to this process are the ubiquitin recognition family of proteins, which include Rpn13, S5a and the UBL-UBA family members hHR23 and hPLIC. To determine how ubiquitin and its chains are recuognized in cells, these researchers have solved the structures of hHR23a, S5a, and Rpn13 alone as well as complexed with ubiquitin. Current studies focus on the mechanisms used by cells to determine the outcome of ubiquitylation and how ubiquitin recognition proteins collaborate towards this agenda. An additional project focuses on how substrate proteins are identified in cells and why this process sometimes goes awry.

Group Members

Xiang Chen, Research Associate
Aaron Ehlinger, Graduate Student
Yang Kang, Postdoctoral Fellow
Fen Liu, Graduate Student
Bala Medicherla, Research Associate
Leah Randles, Graduate Student
William C. Solomon, Supercomputing Institute Undergraduate Intern
Naixia Zhang, Research Assistant Professor