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SUMOylation of synaptic and synapse‐associated proteins: An update

SUMOylation is a post‐translational modification that regulates protein signalling and complex formation by adjusting the conformation or protein–protein interactions of the substrate protein. There is a compelling and rapidly expanding body of evidence that, in addition to SUMOylation of nuclear pr...

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Autores principales: Henley, Jeremy M., Seager, Richard, Nakamura, Yasuko, Talandyte, Karolina, Nair, Jithin, Wilkinson, Kevin A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8218484/
https://www.ncbi.nlm.nih.gov/pubmed/32538470
http://dx.doi.org/10.1111/jnc.15103
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author Henley, Jeremy M.
Seager, Richard
Nakamura, Yasuko
Talandyte, Karolina
Nair, Jithin
Wilkinson, Kevin A.
author_facet Henley, Jeremy M.
Seager, Richard
Nakamura, Yasuko
Talandyte, Karolina
Nair, Jithin
Wilkinson, Kevin A.
author_sort Henley, Jeremy M.
collection PubMed
description SUMOylation is a post‐translational modification that regulates protein signalling and complex formation by adjusting the conformation or protein–protein interactions of the substrate protein. There is a compelling and rapidly expanding body of evidence that, in addition to SUMOylation of nuclear proteins, SUMOylation of extranuclear proteins contributes to the control of neuronal development, neuronal stress responses and synaptic transmission and plasticity. In this brief review we provide an update of recent developments in the identification of synaptic and synapse‐associated SUMO target proteins and discuss the cell biological and functional implications of these discoveries. [Image: see text]
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spelling pubmed-82184842021-06-28 SUMOylation of synaptic and synapse‐associated proteins: An update Henley, Jeremy M. Seager, Richard Nakamura, Yasuko Talandyte, Karolina Nair, Jithin Wilkinson, Kevin A. J Neurochem Reviews SUMOylation is a post‐translational modification that regulates protein signalling and complex formation by adjusting the conformation or protein–protein interactions of the substrate protein. There is a compelling and rapidly expanding body of evidence that, in addition to SUMOylation of nuclear proteins, SUMOylation of extranuclear proteins contributes to the control of neuronal development, neuronal stress responses and synaptic transmission and plasticity. In this brief review we provide an update of recent developments in the identification of synaptic and synapse‐associated SUMO target proteins and discuss the cell biological and functional implications of these discoveries. [Image: see text] John Wiley and Sons Inc. 2020-07-05 2021-01 /pmc/articles/PMC8218484/ /pubmed/32538470 http://dx.doi.org/10.1111/jnc.15103 Text en © 2020 The Authors. Journal of Neurochemistry published by John Wiley & Sons Ltd on behalf of International Society for Neurochemistry https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Reviews
Henley, Jeremy M.
Seager, Richard
Nakamura, Yasuko
Talandyte, Karolina
Nair, Jithin
Wilkinson, Kevin A.
SUMOylation of synaptic and synapse‐associated proteins: An update
title SUMOylation of synaptic and synapse‐associated proteins: An update
title_full SUMOylation of synaptic and synapse‐associated proteins: An update
title_fullStr SUMOylation of synaptic and synapse‐associated proteins: An update
title_full_unstemmed SUMOylation of synaptic and synapse‐associated proteins: An update
title_short SUMOylation of synaptic and synapse‐associated proteins: An update
title_sort sumoylation of synaptic and synapse‐associated proteins: an update
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8218484/
https://www.ncbi.nlm.nih.gov/pubmed/32538470
http://dx.doi.org/10.1111/jnc.15103
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