Synthesis and protein binding studies of a peptide fragment of clathrin assembly protein AP180 bearing an O-linked β-N-acetylglucosaminyl-6-phosphate modification.

Mark E Graham, Robin S Stone, Phillip J Robinson, Richard J Payne

Cell Signalling Unit, Children's Medical Research Institute, Locked Bag 23, Wentworthville, NSW 2145, Australia. mgraham@cmri.org.au

Organic & biomolecular chemistry 2012 Apr 7

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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.

Citation

Mark E Graham, Robin S Stone, Phillip J Robinson, Richard J Payne. Synthesis and protein binding studies of a peptide fragment of clathrin assembly protein AP180 bearing an O-linked β-N-acetylglucosaminyl-6-phosphate modification. Organic & biomolecular chemistry. 2012 Apr 7;10(13):2545-51