Role of myosin motors in the cell.

Schematic showing the highly conserved collection of proteins involved in actomyosin ring assembly. Myosin-II is highlighted.
Contractile ring assembly and constriction visualized by time-lapse fluorescence microscopy of GFP-myosin-II.



Profile

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

Research Description

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.

Schematic showing the highly conserved collection of proteins involved in actomyosin ring assembly. Myosin-II is highlighted.

Contractile ring assembly and constriction visualized by time-lapse fluorescence microscopy of GFP-myosin-II.

Contractile ring assembly and constriction visualized by time-lapse fluorescence microscopy of GFP-myosin-II.

Selected 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.

* indicates equal contribution


Matthew Lord, Ph.D.

Matthew
Lord, Ph.D.

 

802-656-9898

Office: HSRF 108

Lab: HSRF 140

Lab Homepage

Lab Members

   George Murray, Staff
   Luther Pollard, CMB Student

Upcoming Events

  • 5/28/2013 11:30 AM - 12:30 PM
    Davis Auditorium
    TBA
    Dr. Arsalan Syed
  • 6/4/2013 11:30 AM - 12:30 PM
    Davis Auditorium
    Mock predoctoral study section
    Dr. Alan Howe
  • 6/11/2013 11:30 AM - 12:30 PM
    Davis Auditorium
    TBA
    Dr. Ben Green

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