Dr. Reese received a B.S. degree in Molecular Biophysics & Biochemistry from Yale University in 1998. While at Yale, he worked in the laboratory of Dr. Axel Brunger on structural studies of mammalian vesicular transport proteins (SNAPs and SNAREs). After Yale, Dr. Reese spent two years teaching high school science to gifted students with learning disabilities.
Dr. Reese received a Ph.D. in Biophysics in 2006 from the University of California, San Francisco, where he worked jointly in the laboratories of Dr. Frances Brodsky and Dr. Volker Doetsch on the structural basis for the activities of proteins involved in protein trafficking and neuronal signaling. During his postdoctoral work with John Boothroyd at Stanford University, Dr. Reese made the surprising discovery that a family of catalytically inactive kinases, or pseudokinases, are essential to Toxoplasma's ability to cause disease in mice. Dr. Reese went on to demonstrate that these pseudokinases are allosteric inhibitors of the immune-related GTPases, which are critical for the control of a variety of intracellular pathogens.
In the fall of 2013, Dr. Reese joined the faculty in the Department of Pharmacology at UT Southwestern. His lab is focused on determining the many mechanisms by which the ubiquitous intracellular parasite, Toxoplasma gondii, co-opts the signaling networks of its host organisms. His laboratory combines techniques from multiple disciplines: from classical and molecular genetics and cell biology to biophysics and structural biology. This allows the examination of problems at many levels, from the atomic order structures of protein-protein complexes to the analysis of the signatures of evolutionary competition written in the genomes of the parasite and its hosts.
- Yale University (1998), Molecular Biophysics
- Graduate School
- University of California-San F (2006), Biophysics
- Cell signaling, kinases, pseudokinases
- Host-pathogen interaction; co-evolution
- Structural biology
- Rapid identification of protein-protein interfaces for the construction of a complex model based on multiple unassigned signals by using time-sharing NMR measurements.
- Kodama Y, Reese ML, Shimba N, Ono K, Kanamori E, Dötsch V, Noguchi S, Fukunishi Y, Suzuki E, Shimada I, Takahashi H J. Struct. Biol. 2011 Jun 174 3 434-42
- Toxoplasma rhoptry protein 16 (ROP16) subverts host function by direct tyrosine phosphorylation of STAT6.
- Ong YC, Reese ML, Boothroyd JC J. Biol. Chem. 2010 Sep 285 37 28731-40
- A helical membrane-binding domain targets the Toxoplasma ROP2 family to the parasitophorous vacuole.
- Reese ML, Boothroyd JC Traffic 2009 Oct 10 10 1458-70
- The guanylate kinase domain of the MAGUK PSD-95 binds dynamically to a conserved motif in MAP1a.
- Reese ML, Dakoji S, Bredt DS, Dötsch V Nat. Struct. Mol. Biol. 2007 Feb 14 2 155-63
- Fast mapping of protein-protein interfaces by NMR spectroscopy.
- Reese ML, Dötsch V J. Am. Chem. Soc. 2003 Nov 125 47 14250-1
- Clathrin light and heavy chain interface: alpha-helix binding superhelix loops via critical tryptophans.
- Chen CY, Reese ML, Hwang PK, Ota N, Agard D, Brodsky FM EMBO J. 2002 Nov 21 22 6072-82
Interactions Between Toxoplasma Effectors and Host Immune Respones. In Toxoplasma gondii. 2nd edition. K. Kim and L. Weiss (eds.)
Butcher BA, Reese ML, Boothroyd JC, Denkers EY. (2013). London, Academic Press
Honors & Awards
- NSF CAREER Award
- UT Southwestern President's Research Council Distinguished Researcher Award
- NIAID K22 Research Scholar Development Award
Career transition grant (2011-2016)
- American Cancer Society Postdoctoral Research Fellowship
- National Science Foundation Graduate Research Fellow