title: A method to the madness of N-glycan complexity?
abstract: Cell-surface glycoprotein receptors have varying numbers of N-glycan sites. In this issue of Cell, Lau et al. (2007) report that increasing intracellular UDP-GlcNAc leads to increased branching of N-glycans, increased receptor association with cell-surface galectin-3, and enhanced signaling. They also show that the kinetics of this response differ between growth-promoting receptors, which have 8-16 N-glycans, and those that induce growth arrest, which have very few N-glycans, suggesting that hexosamine flux may regulate the transition from growth to arrest.
authors.affiliation: Department of Cell Biology, Albert Einstein College Medicine, New York, NY 10461, USA. stanley@aecom.yu.edu <stanley@aecom.yu.edu>
authors.forename: Pamela
authors.initials: P
authors.lastname: Stanley
mesh_terms: D000818:Animals; D037502:Galectin 3 / Q000378:metabolism; D006031:Glycosylation; D006595:Hexosamines / Q000378:metabolism; D051379:Mice; D017351:N-Acetylglucosaminyltransferases / Q000378:metabolism; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism*; D014537:Uridine Diphosphate N-Acetylglucosamine / Q000378:metabolism
chemical_list: D037502:Galectin 3; D006595:Hexosamines; D011134:Polysaccharides; D014537:Uridine Diphosphate N-Acetylglucosamine; D017351:N-Acetylglucosaminyltransferases