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Super Resolution Microscopy of SUMO Proteins in Neurons
The ubiquitously expressed SUMO proteins regulate a plethora of cellular pathways and processes. While they have a predominantly nuclear localization, extranuclear roles of SUMO isoforms at the synapse have also been described, making SUMOylation one of the major post-translational regulators of ner...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6844275/ https://www.ncbi.nlm.nih.gov/pubmed/31749687 http://dx.doi.org/10.3389/fncel.2019.00486 |
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author | Colnaghi, Luca Russo, Luca Natale, Carmina Restelli, Elena Cagnotto, Alfredo Salmona, Mario Chiesa, Roberto Fioriti, Luana |
author_facet | Colnaghi, Luca Russo, Luca Natale, Carmina Restelli, Elena Cagnotto, Alfredo Salmona, Mario Chiesa, Roberto Fioriti, Luana |
author_sort | Colnaghi, Luca |
collection | PubMed |
description | The ubiquitously expressed SUMO proteins regulate a plethora of cellular pathways and processes. While they have a predominantly nuclear localization, extranuclear roles of SUMO isoforms at the synapse have also been described, making SUMOylation one of the major post-translational regulators of nerve functions. These findings have however recently been challenged, at least for SUMO1, by the analysis of knock-in mice expressing His(6)-HA-SUMO1, where the authors failed to detect the protein at the synapse. In the ongoing dispute, the subcellular distribution in neurons of SUMO2/3 and of the E2 SUMO ligase Ubc9 has not been examined. To investigate whether SUMO proteins do or do not localize at the synapse, we studied their localization in hippocampal primary neurons by super resolution microscopy. We found that SUMO1, SUMO2/3, and Ubc9 are primarily nuclear proteins, which also colocalize partially with pre- and post-synaptic markers such as synaptophysin and PSD95. |
format | Online Article Text |
id | pubmed-6844275 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-68442752019-11-20 Super Resolution Microscopy of SUMO Proteins in Neurons Colnaghi, Luca Russo, Luca Natale, Carmina Restelli, Elena Cagnotto, Alfredo Salmona, Mario Chiesa, Roberto Fioriti, Luana Front Cell Neurosci Neuroscience The ubiquitously expressed SUMO proteins regulate a plethora of cellular pathways and processes. While they have a predominantly nuclear localization, extranuclear roles of SUMO isoforms at the synapse have also been described, making SUMOylation one of the major post-translational regulators of nerve functions. These findings have however recently been challenged, at least for SUMO1, by the analysis of knock-in mice expressing His(6)-HA-SUMO1, where the authors failed to detect the protein at the synapse. In the ongoing dispute, the subcellular distribution in neurons of SUMO2/3 and of the E2 SUMO ligase Ubc9 has not been examined. To investigate whether SUMO proteins do or do not localize at the synapse, we studied their localization in hippocampal primary neurons by super resolution microscopy. We found that SUMO1, SUMO2/3, and Ubc9 are primarily nuclear proteins, which also colocalize partially with pre- and post-synaptic markers such as synaptophysin and PSD95. Frontiers Media S.A. 2019-11-01 /pmc/articles/PMC6844275/ /pubmed/31749687 http://dx.doi.org/10.3389/fncel.2019.00486 Text en Copyright © 2019 Colnaghi, Russo, Natale, Restelli, Cagnotto, Salmona, Chiesa and Fioriti. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Neuroscience Colnaghi, Luca Russo, Luca Natale, Carmina Restelli, Elena Cagnotto, Alfredo Salmona, Mario Chiesa, Roberto Fioriti, Luana Super Resolution Microscopy of SUMO Proteins in Neurons |
title | Super Resolution Microscopy of SUMO Proteins in Neurons |
title_full | Super Resolution Microscopy of SUMO Proteins in Neurons |
title_fullStr | Super Resolution Microscopy of SUMO Proteins in Neurons |
title_full_unstemmed | Super Resolution Microscopy of SUMO Proteins in Neurons |
title_short | Super Resolution Microscopy of SUMO Proteins in Neurons |
title_sort | super resolution microscopy of sumo proteins in neurons |
topic | Neuroscience |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6844275/ https://www.ncbi.nlm.nih.gov/pubmed/31749687 http://dx.doi.org/10.3389/fncel.2019.00486 |
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