A1 Refereed original research article in a scientific journal
Analysis of SUMO1-conjugation at synapses
Authors: Daniel JA, Cooper BH, Palvimo JJ, Zhang FP, Brose N, Tirard M
Publisher: ELIFE SCIENCES PUBLICATIONS LTD
Publication year: 2017
Journal: eLife
Journal name in source: ELIFE
Journal acronym: ELIFE
Article number: ARTN e26338
Volume: 6
First page : 1
Last page: 36
Number of pages: 36
ISSN: 2050-084X
DOI: https://doi.org/10.7554/eLife.26338
Web address : https://research.utu.fi/converis/portal/Publication/26330217
Self-archived copy’s web address: https://research.utu.fi/converis/portal/detail/Publication/26330217
SUMO1-conjugation of proteins at neuronal synapses is considered to be a major post-translational regulatory process in nerve cell and synapse function, but the published evidence for SUMO1-conjugation at synapses is contradictory. We employed multiple genetic mouse models for stringently controlled biochemical and immunostaining analyses of synaptic SUMO1-conjugation. By using a knock-in reporter mouse line expressing tagged SUMO1, we could not detect SUMO1-conjugation of seven previously proposed synaptic SUMO1-targets in the brain. Further, immunostaining of cultured neurons from wild-type and SUMO1 knock-out mice showed that anti-SUMO1 immunolabelling at synapses is non-specific. Our findings indicate that SUMO1-conjugation of synaptic proteins does not occur or is extremely rare and hence not detectable using current methodology. Based on our data, we discuss a set of experimental strategies and minimal consensus criteria for the validation of SUMOylation that can be applied to any SUMOylation substrate and SUMO isoform.
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