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Issue 13, 2012
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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

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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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Publication details

The article was received on 20 Dec 2011, accepted on 01 Feb 2012 and first published on 03 Feb 2012


Article type: Communication
DOI: 10.1039/C2OB07139H
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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