Mechanisms for regulation via localization: Analysis of subcellular localization of polylactosamine-synthesizing glycosyltransferases

BIOL 131

Peter L. Lee, plee82@stanford.edu1, Julie A. Theriot, theriot@stanford.edu2, and Jennifer J. Kohler, jjkohler@stanford.edu1. (1) Department of Chemistry, Stanford University, 380 Roth Way Drive, Keck Science Bldg, Rm 363, Stanford, CA 94305-5080, (2) Department of Biochemistry, Stanford University School of Medicine, 279 West Campus Drive, Stanford, CA 94305-5307
Enzyme localization has been demonstrated to be essential to enzyme function. The three-dimensional architecture of the Golgi and the heterogeneous glycans that it produces are indicative of a loosely regulated system susceptible to stochastic processes such as changes in enzyme localization. Poly-N-acetyllactosamine (polyLacNAc) is a polymer of galactose and N-acetylglucosamine (GlcNAc) that can be found in both N-linked and O-linked glycans. polyLacNAc is synthesized by the alternate actions of a β1,3 GlcNAc-transferase (β3GlcNAcT) and a β1,4 galactosyltransferase (β4GalT). The β3GlcNAcT and β4GalT gene families each contain multiple members that exhibit tissue-specific expression patterns. We are investigating the physical and functional association of various pairs of β3GlcNAcT and β4GalT enzymes. We are also identifying the features that cause β3GlcNAcT and β4GalT enzymes to localize to specific sites within the secretory pathway. We hope to correlate subcellular glycosyltransferase localization with global carbohydrate expression patterns.
 

Chemistry and Metabolism
4:30 PM-6:30 PM, Tuesday, 12 September 2006 Moscone Center -- Hall D, Poster

Division of Biological Chemistry

The 232nd ACS National Meeting, San Francisco, CA, September 10-14, 2006