Matthew Lord, Ph.D.
1991-94: BSc Microbiology, University of Sheffield, UK
1994-98: DPhil Biochemistry, University of Oxford, UK
1998-2001: HF Long-term Fellow, Harvard Univ, USA
2001-05: Post-doctoral Fellow, Yale University, USA
2006-present: Assistant Professor, UVM
The long-term goal of our research lies in understanding how the actin-based myosin motors operate in the cell. Our lab focuses on the roles of myosin-I (in endocytosis), myosin-II (in cytokinesis), and myosin-V (in organelle and mRNA transport).
We employ both the fission and budding yeasts as models, taking advantage of the versatile molecular genetics and cell biology approaches on offer in these systems. Current interests lie in regulation of myosins by i) modification of the actin track, and ii) UCS domain proteins.
We utilize a variety of techniques including molecular biology, yeast genetics, and live cell imaging to track actomyosin dynamics (at contractile rings, endocytic patches, and during intracellular transport). We have optimized the purification of myosin-I, -II, and -V from yeast, allowing us to complement our in vivo approaches with biochemical assays to dissect mechanisms of regulation. Knowing how myosin motors are controlled in cells represents an important step in understanding the actomyosin-dependent processes governing cell proliferation and motility in cancer cells.
Schematic showing the highly conserved collection of proteins involved in actomyosin ring assembly. Myosin-II is highlighted.
Faculty Highlighted Publications
Pollard, L. W., Onishi, M., Pringle, J. R., and Lord, M. Fission yeast Cyk3p is a transglutaminase-like protein that participates in cytokinesis and cell morphogenesis. Mol. Biol. Cell, 2012, 23, 2433-2444.
Kovar, D. R., Sirotkin, V., and Lord, M. ThreeÂ’s company: the fission yeast actin cytoskeleton. Trends Cell Biol., 2011, 21, 177-187.
Stark, B. C., Wen, K.-K., Allingham, J. S., Rubenstein, P. A., and Lord, M. Functional adaptation between yeast actin and its cognate myosin motors. J. Biol. Chem., 2011, 286, 30384-30392.
Sammons, M. R., James, M. L., Clayton, J. E., Sladewski, T. E., Sirotkin, V., and Lord, M. A calmodulin-related light chain from fission yeast that functions with myosin-I and PI 4-kinase. J. Cell Sci., 2011, 124, 2466-2477
Clayton, J. E., Sammons, M. R., Stark, B. C., Hodges, A. R., and Lord, M. Differential regulation of unconventional fission yeast myosins via the actin track. Curr. Biol., 2010, 20, 1423-1431.
Stark, B. C., Sladewski, T. E., Pollard, L. W. and Lord, M. Tropomyosin and myosin-II cellular levels promote actomyosin interactions and contractile ring assembly in fission yeast. Mol. Biol. Cell, 2010, 21, 989-1000.
Clayton JE, Sammons MR, Stark BC, Hodges AR, and Lord M. Differential regulation of unconventional fission yeast myosins via the actin track. Curr. Biol. 2010; 20: 1423-1431.
Lord M. Cytokinesis mechanisms in yeast. Nature Education. 2010;3(9):53.
Bookwalter CS, Lord M, and Trybus KM. Essential features of the class V myosin from budding yeast for ASH1 and mRNA transport. Mol. Biol. Cell. 2009;20:3414-3421.
Sladewski TE, Previs MJ, and Lord M. Regulation of fission yeast myosin-II function and contractile ring dynamics by regulatory light chain and heavy chain phosphorylation. Mol. Biol. Cell. 2009;20:3941-3952.
Lord M, Sladewski TE, and Pollard TD. Yeast UCS proteins promote actomyosin interactions and limit myosin turnover in cells. Proc. Natl. Acad. Sci. USA. 2008;105:8014-8019.