Analysis of SUMO-1 modification of neuronal proteins containing consensus SUMOylation motifs

NEUROSCIENCE LETTERS

卷:436

Article

Wilkinson, Kevin A.¹  Nishimune, Atsushi¹  Henley, Jeremy M.¹ 

[1] Univ Bristol, Sch Med Sci, MRC, Ctr Synapt Plast,Dept Anat, Bristol BS8 1TD, Avon, England

关键词: SUMO;    posttranslational modification;    SUMOylation;    metabotropic glutamate receptors;    group III mGIuRs;    kainate receptor;    GluR7;    synaptic protein;   

DOI  :  10.1016/j.neulet.2008.03.029

来源: Elsevier

【 摘 要 】

SUMOylation is emerging as an important mechanism for modulating protein function in many cell types. A large variety of proteins have been proposed as SUMO targets based on the presence of a consensus SUMOylation core motif (psi-K-x-D/E). In neurons these include multiple synaptic proteins but it has not been established whether proteins carrying this motifare SUMOylated either in vitro or in vivo. Here we use a bacterial SUMOylation assay to systematically test for SUMO-1 modification of a selection of neuronal proteins containing one or more amino acid sequences predicted as high-probability SUMOylation sites in computer-based searches. Of the 39 proteins analysed only 14 sites were posttranslationally modified by SUMO-1, including the group III metabotropic glutamate receptors and the kainate receptor subunit GIuR7. These results identify new candidate proteins that may be involved in the SUMO regulation of synaptic activity and also demonstrate that the presence of the psi-K-x-D/E motif is not sufficient to indicate that a protein can be SUMOylated in this bacterial system. (c) 2008 Elsevier Ireland Ltd. All rights reserved.

【 授权许可】

Free