title: Synthesis and protein binding studies of a peptide fragment of clathrin assembly protein AP180 bearing an O-linked β-N-acetylglucosaminyl-6-phosphate modification.
abstract: A novel post-translational modification of threonine, β-N-acetylglucosaminyl-phosphate, was recently discovered on assembly protein AP180, a protein which plays a crucial role in clathrin coated vesicle formation in synaptic vesicle endocytosis (SVE). Herein, we report studies aimed at probing the effect of this modification on binding to proteins in rat brain lysate using pull down experiments with peptide fragments of AP180.
authors.affiliation: Cell Signalling Unit, Children's Medical Research Institute, Locked Bag 23, Wentworthville, NSW 2145, Australia. mgraham@cmri.org.au
authors.forename: Mark E
authors.initials: ME
authors.lastname: Graham
authors.forename: Robin S
authors.initials: RS
authors.lastname: Stone
authors.forename: Phillip J
authors.initials: PJ
authors.lastname: Robinson
authors.forename: Richard J
authors.initials: RJ
authors.lastname: Payne
mesh_terms: D000107:Acetylation; D005944:Glucosamine / Q000031:analogs & derivatives* / Q000737:chemistry; D019298:Glucose-6-Phosphate / Q000031:analogs & derivatives* / Q000737:chemistry; D006020:Glycopeptides / Q000737:chemistry; D015394:Molecular Structure; D034041:Monomeric Clathrin Assembly Proteins / Q000737:chemistry*; D010446:Peptide Fragments / Q000138:chemical synthesis*
chemical_list: D006020:Glycopeptides; D034041:Monomeric Clathrin Assembly Proteins; D010446:Peptide Fragments; C439023:clathrin assembly protein AP180; C001293:glucosamine 6-phosphate; D019298:Glucose-6-Phosphate; D005944:Glucosamine