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Fred Mast

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The cell may be the basic building block of life, but Mast is exploring its complexity. His research seeks to better understand the intricacies of cells and to identify the ways in which proteins are trafficked through cells. Mast hopes to enhance fundamental knowledge of how proteins are transported to their site of action in normal cell physiology, and how new therapies could be devised to avoid altered protein trafficking that can lead to disease.

Fred Mast

Department of Cell Biology

fmast@ualberta.ca
Curriculum Vitae

  • Ph.D. candidate

  • Molecular mechanisms that direct the formation of peroxisomes from the ER and govern peroxisomal inheritance from mother cell to daughter cells
  • Application of advanced imaging techniques and procedures to the study of living cellular phenomena
  • Systems biology and bioinformatic approaches to studying peroxisome biogenesis

  • President’s Doctoral Prize of Distinction, University of Alberta, 2010
  • President’s Doctoral Prize of Distinction, University of Alberta, 2009.
  • Vanier Canada Graduate Scholar, Canadian Institutes of Health Research, 2009-2012
  • Alberta Heritage Foundation for Medical Research Studentship, Alberta Heritage Foundation for Medical Research, 2009-2012.
  • Beyond These Halls – Community Service Recognition, University of Alberta Senate, 2008.
  • Microscopy image published in the Howard Hughes Medical Institute Bulletin, Spring 2008.
  • Graduate Student Scholarship, Province of Alberta, 2008.
  • 75th Anniversary Award, Faculty of Medicine and Dentistry, University of Alberta, 2008.
  • Walter H Johns Graduate Fellowship, University of Alberta, 2007.
  • Frederick Banting and Charles Best Canada Graduate Scholarship – Master’s, Canadian Institutes of Health Research, 2007-2008.

http://hdl.handle.net/10402/era.17170

Subject areas and related deposits

  • Cell cycle/physiology

    • Myosin-driven peroxisome partitioning in S. cerevisiae.

      In Saccharomyces cerevisiae, the class V myosin motor Myo2p propels the movement of most organelles. We recently identified Inp2p as the peroxisome-specific receptor for Myo2p. In this study, we delineate the region of Myo2p devoted to binding peroxisomes. Using mutants of Myo2p specifically impaired in peroxisome binding, we dissect cell cycle–dependent and peroxisome partitioning–dependent mechanisms of Inp2p regulation. We find that although total Inp2p levels oscillate with the cell cycle, Inp2p levels on individual peroxisomes are controlled by peroxisome inheritance, as Inp2p aberrantly accumulates and decorates all peroxisomes in mother cells when peroxisome partitioning is abolished. We also find that Inp2p is a phosphoprotein whose level of phosphorylation is coupled to the cell cycle irrespective of peroxisome positioning in the cell. Our findings demonstrate that both organelle positioning and cell cycle progression control the levels of organelle-specific receptors for molecular motors to ultimately achieve an equidistribution of compartments between mother and daughter cells.

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  • Peroxisomes