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Home » Faculty Listings » Mark Hannink
Professor of Biochemistry
Basil O'Conner Scholar, March of Dimes, 1991-93
Electronic submission is encouraged, e-mail to biochemsearch@missouri.edu
Applicants should send CV and names of two references to:
Dr. Mark Hannink
Postdoctoral Application
Biochemistry
440E Bond Life Sciences Center
University of Missouri-Columbia
Columbia, MO 65211
The BTB-Kelch substrate adaptor family in development, oncogenesis and neurodegeneration.
Mark Hannink
Professor of Biochemistry
Associate Director, Fellowships and Education, Life Sciences Center
| Email: | hanninkm@missouri.edu |
 |
| Phone: | (573) 882-7971 | |
| Lab: | (573) 882-1378 | |
| Fax: | (573) 884-3087 | |
| Office: | 440E Bond Life Sciences Center | |
| Mailing Address: |
Biochemistry
440E Bond Life Sciences Center University of Missouri-Columbia Columbia, MO 65211 |
|
| Research Areas: |
The BTB-Kelch substrate adaptor family in development, oncogenesis and neurodegeneration. |
Educational Background
| BS | Calvin College | Grand Rapids, Mich. | Chemistry | |
| MS | University of Washington | Seattle, Wash. | Organic Chemistry | |
| PhD | University of California-San Diego | La Jolla, Calif. | Biochemistry |
Notable Honors and Service
Basil O'Conner Scholar, March of Dimes, 1991-93
Research Description
Dr. Hannink's research focuses on the molecular and cellular mechanisms of intracellular signal transduction, particularly the signaling mechanisms that enable cells to sense and respond to oxidative stress. Dr. Hannink's laboratory has identified an E3 ubiquitin ligase complex that is responsive to oxidative stress. The major substrate of this ubiquitin ligase complex is the Nrf2 transcription factor, which controls a transcriptional program that enables cells to neutralize reactive molecules and maintain cellular redox homeostasis. We utilize a variety of experimental approaches, including structural, molecular, biochemical and cell biology. We have identified a BTB-Kelch protein termed Keap1 as the substrate adaptor protein that targets Nrf2 for ubiquitin-dependent degradation, we have determined the structure of the substrate binding domain of Keap1 and we have identified redox-sensitive cysteine residues in Keap1 that are critically required for sensing oxidative stress. The BTB-Kelch protein family constitutes a large family of substrate adaptor proteins encoded by the human genome and we are currently investigating the role of other BTB-Kelch proteins in neurodegenerative, neuromuscular and cardiovascular diseases. We collaborate with a number of other research groups across campus, including x-ray crystallographers, radiologists interested in non-invasive imaging of cancer, neurobiologists interested in Alzheimer’s disease, and reproductive biologists working to unlock the therapeutic potential of human embryonic stem cells. Dr. Hannink has trained 9 graduate students and 3 postdoctoral fellows, served on more than 60 doctoral program committees, and has been extensively involved in both graduate and medical educational activities.
Selected Publications
Zhang DD, Hannink M. Distinct cysteine residues in Keap1 are required for Keap1-dependent degradation of Nrf2 and for stabilization of Nrf2 by chemopreventive agents. Mol Cell Biol, 2003, 23: 8137-8151. [full paper]
Zhang DD, Lo SC, Cross JV, Templeton DJ, and Hannink M. Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. Mol Cell Biol 2004, 24: 10941-10953. [full paper]
Li X, Zhang DD, Hannink M, and Beamer LJ. Crystal structure of the Kelch domain of Keap1: A structural model for the substrate binding domain of BTB-Kelch substrate adaptor proteins. J Biol Chem, 2004, 279: 54750-54758. [full paper]
Zhang DD, Lo SC, Habib GM, Lieberman MW, and Hannink M. Ubiquitination of Keap1, a BTB-Kelch substrate adaptor for Cul3, targets Keap1 for degradation by a proteosome-independent pathway. J. Biol Chem, 2005, 280: 30091-9. [full paper]
Lo SC and Hannink M. Substrate adaptor recycling is required for efficient Keap1-dependent ubiquitination of Nrf2. Mol Cell Biol 2006, 26: 1235-1244. [full paper]
Lo SC, Li X, Henzl MT, Beamer LJ, Hannink M. Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling. EMBO J, 2006, 25: 3605-17. [full paper]
Lo SC, Hannink M. PGAM5, a Bcl-XL-interacting protein, is a novel substrate for the redox-regulated Keap1-dependent ubiquitin ligase complex. J Biol Chem. 2006 Oct 17; (Epub ahead of print) [full paper]
Employment Opportunities
Electronic submission is encouraged, e-mail to biochemsearch@missouri.edu
Applicants should send CV and names of two references to:
Dr. Mark Hannink
Postdoctoral Application
Biochemistry
440E Bond Life Sciences Center
University of Missouri-Columbia
Columbia, MO 65211
The BTB-Kelch substrate adaptor family in development, oncogenesis and neurodegeneration.
Affiliated with the College of Agriculture, Food and Natural Resources and the School of Medicine