Research Summary The focus of my laboratory is to understand the processes involved in the maturation and degradation of proteins that traverse the secretory pathway in the living cell. Protein maturation is a highly assisted process enlisting the help of many cellular factors. We are particularly interested in understanding the role of co-translational folding and modifications that occur in the endoplasmic reticulum, and the involvement of molecular chaperones in these processes. The cell also possesses a quality control system that helps to ensure that only properly folded and assembled proteins are generated. Proteins that are unable to reach their native conformation are targeted for destruction. As our knowledge of protein maturation and quality control increases, it has become clear that a number of common human genetic diseases involve protein maturation defects including cystic fibrosis, albinism, melanoma and heart disease. Current model proteins that our laboratory studies include: tyrosinase, the key protein in melanin synthesis or cellular pigmentation; and the flu viral glycoprotein, hemagglutinin. We employ a variety of cell biololgical, biochemical, and molecular biological approaches to study the maturation and degradation of membrane glycoproteins using cell-free asssays, isolated organelles and live cells.
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Characterization of early EDEM1 maturation events and their functional implications (with J. H. Cormier and T. Tamura), The Journal of Biological Chemistry (2011)
The endoplasmic reticulum (ER) quality control factor EDEM1 associates with a number of ER proteins...
The SV40 late protein VP4 is a viroporin that forms pores to disrupt membranes for viral release (with S. Raghava, K. M. Giorda, F. B. Romano, and A. P. Heuck), PLoS Pathogens (2011)
Nonenveloped viruses are generally released by the timely lysis of the host cell by a...
Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum (with Bradley R. Pearse), Biochim Biophys Acta (2010)
Eukaryotic secretory pathway cargo fold to their native structures within the confines of the endoplasmic...
The role of UDP-Glc:glycoprotein glucosyltransferase 1 in the maturation of an obligate substrate prosaposin (with R. J. Kaufman, G. A. Grabowski, J. C. Sunryd, T. Tamura, and B. R. Pearse), Journal of Cell Biology (2010)
An endoplasmic reticulum (ER) quality control system assists in efficient folding and disposal of misfolded...