Interdisciplinary Life Science - PULSe Great research is a matter of choice

Mark C. Hall

Mark C. Hall Profile Picture

Assistant Professor of Biochemistry
Ph.D. University of North Carolina, Chapel Hill, 1998


Contact Info:

mchall@purdue.edu
765-494-0714


Training Group(s):
Molecular Signaling and Cancer Biology


Current Research Interests:

The cell division cycle in eukaryotic organisms is a complex series of strictly regulated events that ensures 1) that the genome is replicated accurately and 2) that complete copies of the genome are faithfully distributed to the daughter cells. Cancer ultimately results from loss of control over the cell division cycle, and therefore a clear understanding of the molecular processes that dictate cell cycle progression is essential to a fundamental understanding of carcinogenesis. In all eukaryotic cells the sequential stages of the cell cycle are regulated by two important post-translational mechanisms: reversible protein phosphorylation, and ubiquitin-dependent proteolysis. These processes are interdependent, and together they drive the cell cycle forward with the proper order and timing.

Our lab is interested in how ubiquitin-dependent proteolysis directed by the anaphase-promoting complex (APC) is used to regulate cell division in the budding yeast, Saccharomyces cerevisiae. Budding yeast are easy to work with and manipulate genetically, and therefore make a highly attractive and suitable model organism for studying the evolutionarily conserved cell cycle and understanding its relationship to cancer in humans. The APC is a large, highly conserved, multisubunit enzyme that catalyzes the polyubiquitylation of specific substrate proteins at specific points during the cell cycle. The polyubiquitin tags serve as markers for substrates to be destroyed by the proteasome. By this mechanism, the cell cycle progresses from one stage to the next by the selective and irreversible elimination of inhibitory proteins. Understanding the exquisite selectivity and timing of APC activity is a fascinating area of research and a major focus of our lab. Because one form of the APC is now thought to act as a tumor suppressor, this work is also important for defining how defective APC activity and regulation are related to cancer in humans.



Selected Publications:

Choi E., Dial J.M., Jeong D., and Hall M.C. (2008). Unique D-box and KEN-box sequences limit ubiquitination of Acm1 and promote pseudosubstrate inhibition of the anaphase-promoting complex. J. Biol. Chem. 283(35): 23701-10.

Hall M.C., Jeong D., Henderson J.T., Choi E., Bremmer S.C., Iliuk A.B., and Charbonneau H. (2008). Cdc28 and Cdc14 control stability of the anaphase-promoting complex inhibitor Acm1. J. Biol. Chem. 283(16): 10396-407.

Martinez, J.S., Jeong, D-E., Choi, E., Billings, B.M., and Hall, M.C. (2006). Acm1 is a negative regulator of the Cdh1-dependent anaphase-promoting complex/cyclosome in budding yeast. Mol Cell Biol 26(24): 9162-76.

Hall, M.C., Warren, E.N., and Borchers, C.H. (2004) Multi-kinase phosphorylation of the APC/C activator Cdh1 revealed by mass spectrometry. Cell Cycle 3(10): 1278-84.

Hall,M.C., Torres, M.P., Schroeder, G., and Borchers, C.H. (2003). Mnd2 and Swm1 are core subunits of the Saccharomyces cerevisiae anaphase-promoting complex. J. Biol. Chem. 278: 16698-705.

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