Mark C. Hall

Mark C. Hall Profile Picture

Associate 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

Active Mentor - currently hosting PULSe students for laboratory rotations and recruiting PULSe students into the laboratory; serves on preliminary exam committees

Current Research Interests:

Research in the Hall lab currently focuses on the regulation of mitosis by post-translational processes, including dynamic phosphorylation and ubiqutin-mediated protein degradation. One current project is studying mechanisms of anaphase-promoting complex function. The anaphase-promoting complex is a large E3 ubiquitin ligase that controls the metaphase-anaphase transition, mitotic exit, and G1 phases of the cell cycle among other things. It is the indirect target of existing cancer chemotherapies like taxol and an attractive target for development of new chemotherapies. Our primary interest is understanding how this enzyme is regulated and how it recognizes the correct substrates at the right time to promote their degradation. A second project focuses on characterizing the phosphatases responsible for completing mitosis and cytokinesis during the eukaryotic cell cycle. Much work has focused on understanding the kinases that control cell division but much less is known about their counteracting phosphatases. We are interested in understanding how multiple phosphatases with distinct specificities act together to coordinate mitotic exit and cytokinesis, and maintain genome stability.

Selected Publications:

Powers BL, and Hall, MC (2017). Re-evaluating the role of Cdc14 phosphatase in reversal of Cdk phosphorylation during mitotic exit. J Cell Sci. 130: 2673-2681. PMID: 28663385

Qin L, Guimarães DS, Melesse M, and Hall MC (2016). Substrate recognition by the Cdh1 destruction box receptor is a general requirement for APC/C^Cdh1-mediated proteolysis. J Biol Chem 291:15564-74. PMID: 27226622

Li C, Melesse M, Zhang S, Hao C, Wang C, Zhang H, Hall MC, Xu JR (2015). FgCDC14 regulates cytokinesis, morphogenesis, and pathogenesis in Fusarium graminearum. Mol Microbiol 98(4):770-86. PMID: 26256689

Eissler CL, Mazón G, Powers BL, Savinov SB, Symington LL, and Hall MC (2014). The Cdk/Cdc14 module controls activation of the Yen1 Holliday junction resolvase to promote genome stability. Mol Cell 54: 80-93. PMID: 24631283

Melesse M, Choi E, Hall H, Walsh MJ, Geer MA, and Hall MC (2014). Timely activation of budding yeast APCCdh1 involves degradation of its inhibitor, Acm1, by an unconventional proteolytic mechanism. PLoS ONE 9(7): e103517. PMID: 25072887

Martinez JS, Hall H, Bartolowits MD, and Hall MC (2012). Acm1 contributes to nuclear positioning by inhibiting Cdh1-substrate interactions. Cell Cycle, 11(2): 384-394. PMID: 22189709

Bremmer SC, Hall H, Martinez JS, Eissler CL, Hinrichsen T, Rossie S, Parker LL, Hall MC*, and Charbonneau H (2012). Cdc14 phosphatases preferentially dephosphorylate a subset of cyclin-dependent kinase (Cdk) sites containing phosphoserine. J. Biol. Chem. 287(3): 1662-1669. PMID: 22117071

Eissler CL, Bremmer SC, Martinez JS, Parker LL, Charbonneau H, and Hall MC (2011). A general strategy for studying multi-site protein phosphorylation using label-free selected reaction monitoring mass spectrometry. Anal. Biochem. 418: 267-275. PMID: 21810403

Balasubramaniam D, Eissler CL, Stauffacher CV, and Hall MC (2010). Use of selected reaction monitoring data for label-free quantification of protein modification stoichiometry. Proteomics 10: 4301-4305. PMID: 21046619

Choi E, Dial JM, Jeong D, and Hall MC (2008). Unique D-box and KEN-box sequences limit ubiquitination of Acm1 and promote pseudosubstrate inhibition of the anaphasepromoting complex. J. Biol. Chem. 283(35): 23701-23710. PMID: 18596038

Martinez JS, Jeong D, Choi E, Billings BM, and Hall MC (2006). Acm1 is a negative regulator of the Cdh1-dependent anaphase-promoting complex/cyclosome in budding yeast. Mol. Cell. Biol. 26(24): 9162-9176. PMID: 17030612

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