The broad interest of the laboratory is protein trafficking within the cell and the assembly of organelles. We have focused on the biogenesis of peroxisomes and lipid bodies in yeast. Peroxisomes are found in virtually every eukaryote and catalyze many essential reactions for the organism. Humans who cannot properly assemble peroxisomes are born, miraculously, but die early in childhood as several organ systems fail. It is thus clinically important to understand how this organelle is normally assembled. Yeast is a good model system for this purpose.
Past work has focused on understanding the targeting and assembly of peroxisomal matrix and membrane proteins. Recently we have begun to explore the relationship of peroxisomes and mitochondria to lipid bodies. Lipid bodies store triglycerides and sterol esters, while peroxisomes and mitochondria (in higher eukaryotes) degrade fatty acids derived from these neutral lipids. We have recently found evidence that the physical association of peroxisomes with lipid bodies couples the hydrolysis of neutral lipids with the oxidation of the resulting fatty acids. We believe this may have fundamental importance in energy homeostasis in the cell, a process that goes awry in several diseases including diabetes, heart disease and obesity.
Current efforts in the lab are directed toward understanding the functional relationship among these organelles, as well as understanding the biogenesis of lipid bodies. We have embarked on several screening projects to identify genes involved in peroxisome-mediated fatty acid production, peroxisome-lipid body association, and lipid body biogenesis.
Most recently, as a result of a genomic screen for lipid body morphologies, we identified seipin, a protein responsible for lipodystrophy if mutated, leading to diabetes and other complications in affected patients. In yeast we showed that seipin is involved in lipid body maintenance and/or assembly.
RESEARCH INTERESTS
Protein trafficking
Peroxisomes
Yeast cell biology
Membrane structure
Lipid bodies
RECENT PUBLICATIONS
Leon, S., Goodman, J.M., Subramani, S., "Uniqueness of the mechanism of protein import into the peroxisome matrix: transport of folded, co-factor-bound and oligomeric proteins by shuttling receptors" Biochim Biophys Acta, 1763:1552-1564, December 2006
Joel M. Goodman, "Structure, Function and Biogenesis of Peroxisomes" Encylclopedia of Molecular Cell Biology and Molecular Medicine, 2nd edition, Volume 13 (Sex-Sync):607-635, 2005
Binns, D.D., Januszewski, T.C., Chen, Y., Hill, J.J., Markin, V.S., Zhao, Y., Gilpin, C.J., Chapman, K.D., Anderson, R.G.W., and Goodman, J.M., "An intimate collaboration between peroxisomes and lipid bodies" J. Cell Biol., 173:719-731, June 2006
Wang, X., McMahon, M.A., Shelton, S.N., Nampaisansuk, M., Ballard, J.L., and Goodman, J.M., "Multiple targeting modules on peroxisomal proteins are not redundant: discrete functions of targeting signals within Pmp47 and Pex8p" Mol. Biol. Cell, 15:1702-1710, 2004
Shelton, S.N., Barylko, B., Binns, D.D., Horazdovsky, B.F., Albanesi, J.P., and Goodman, J.M., "Saccharomyces cerevisiae contains a Type II phosphatidylinositol 4-kinase" Biochem J., 371:553-540, 2003
SIGNIFICANT PUBLICATIONS
Binns, D.D., Januszewski, T.C., Chen, Y., Hill, J.J., Markin, V.S., Zhao, Y., Gilpin, C.J., Chapman, K.D., Anderson, R.G.W., and Goodman, J.M., "An intimate collaboration between peroxisomes and lipid bodies" J. Cell Biol., 173:719-731, June 2006
Wang, X., Unruh, M.J., and Goodman, J.M., "Discrete targeting signals direct Pmp47 to oleate-induced peroxisomes in Saccharomyces cerevisiae" J. Biol. Chem., 276:10897-10905, 2001
Dyer, J.M., McNew, J.A. and Goodman, J.M., "The sorting sequence of the peroxisomal integral membrane protein PMP47 is contained within a hydrophilic loop" J. Cell Biol., 133:269-280, 1996
Marshall, P.A., Dyer, J.M., Quick, M.E., and Goodman, J.M., "Redox-sensitive homodimerization of peroxisomal Pmp27: A proposed mechanism to regulate organellar division" J. Cell Biol., 135:123-137, 1996
McNew, J.M., Goodman, J.M., "An oligomeric protein is imported into peroxisomes in vivo" J. Cell Biol., 127:1245-1257, 1994
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