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Issue 13, 2012
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Synthesis and protein binding studies of a peptide fragment of clathrin assemblyprotein 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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Article information


Submitted
20 Dec 2011
Accepted
01 Feb 2012
First published
03 Feb 2012

Org. Biomol. Chem., 2012,10, 2545-2551
Article type
Communication

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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