Issue 13, 2012
From the journal:

Organic & Biomolecular Chemistry

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

Mark E. Graham,*a   Robin S. Stone,ab   Phillip J. Robinsona  and  Richard J. Payne*b  

* Corresponding authors

a Cell Signalling Unit, Children's Medical Research Institute, Locked Bag 23, Wentworthville, NSW 2145, Australia
E-mail: mgraham@cmri.org.au
Fax: +61 2 9687 2120
Tel: +61 2 9687 2800

b School of Chemistry, The University of Sydney, NSW 2006, Australia
E-mail: richard.payne@sydney.edu.au
Fax: +61 2 9351 3329
Tel: +61 2 9351 5877

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.

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

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Article information

DOI
https://doi.org/10.1039/C2OB07139H
Article type
Communication
Submitted
20 Dec 2011
Accepted
01 Feb 2012
First published
03 Feb 2012

Org. Biomol. Chem., 2012,10, 2545-2551

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

M. E. Graham, R. S. Stone, P. J. Robinson and R. J. Payne, Org. Biomol. Chem., 2012, 10, 2545 DOI: 10.1039/C2OB07139H

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