Sumoylation in synaptic function and dysfunction

Sumoylation has recently emerged as a key post-translational modification involved in many, if not all, biological processes. Small Ubiquitin-like MOdifiers (SUMOs) polypeptides are covalently attached to specific lysine residues of target proteins through a dedicated enzymatic pathway. Disruption o...
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Gespeichert in:

Autor*in:	Lenka eSCHOROVA [verfasserIn] Stéphane eMARTIN [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2016

Schlagwörter:	Sumoylation synapse post-translational modification SUMO DeSUMOylation

Übergeordnetes Werk:	In: Frontiers in Synaptic Neuroscience - Frontiers Media S.A., 2011, 8(2016)
Übergeordnetes Werk:	volume:8 ; year:2016

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3389/fnsyn.2016.00009

Katalog-ID:	DOAJ022287256

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language	English
source	In Frontiers in Synaptic Neuroscience 8(2016) volume:8 year:2016
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topic_facet	Sumoylation synapse post-translational modification SUMO DeSUMOylation Neurosciences. Biological psychiatry. Neuropsychiatry
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container_title	Frontiers in Synaptic Neuroscience
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callnumber-first	R - Medicine
author	Lenka eSCHOROVA
spellingShingle	Lenka eSCHOROVA misc RC321-571 misc Sumoylation misc synapse misc post-translational modification misc SUMO misc DeSUMOylation misc Neurosciences. Biological psychiatry. Neuropsychiatry Sumoylation in synaptic function and dysfunction
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topic_title	RC321-571 Sumoylation in synaptic function and dysfunction Sumoylation synapse post-translational modification SUMO DeSUMOylation
topic	misc RC321-571 misc Sumoylation misc synapse misc post-translational modification misc SUMO misc DeSUMOylation misc Neurosciences. Biological psychiatry. Neuropsychiatry
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title	Sumoylation in synaptic function and dysfunction
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title_sort	sumoylation in synaptic function and dysfunction
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title_auth	Sumoylation in synaptic function and dysfunction
abstract	Sumoylation has recently emerged as a key post-translational modification involved in many, if not all, biological processes. Small Ubiquitin-like MOdifiers (SUMOs) polypeptides are covalently attached to specific lysine residues of target proteins through a dedicated enzymatic pathway. Disruption of the SUMO enzymatic pathway in the developing brain leads to lethality indicating that this process exerts a central role during embryonic and post-natal development. However, little is still known regarding how this highly dynamic protein modification is regulated in the mammalian brain despite an increasing number of data implicating sumoylated substrates in synapse formation, synaptic communication and plasticity. The aim of this review is therefore to briefly describe the enzymatic SUMO pathway and to give an overview of our current knowledge on the function and dysfunction of protein sumoylation at the mammalian synapse.
abstractGer	Sumoylation has recently emerged as a key post-translational modification involved in many, if not all, biological processes. Small Ubiquitin-like MOdifiers (SUMOs) polypeptides are covalently attached to specific lysine residues of target proteins through a dedicated enzymatic pathway. Disruption of the SUMO enzymatic pathway in the developing brain leads to lethality indicating that this process exerts a central role during embryonic and post-natal development. However, little is still known regarding how this highly dynamic protein modification is regulated in the mammalian brain despite an increasing number of data implicating sumoylated substrates in synapse formation, synaptic communication and plasticity. The aim of this review is therefore to briefly describe the enzymatic SUMO pathway and to give an overview of our current knowledge on the function and dysfunction of protein sumoylation at the mammalian synapse.
abstract_unstemmed	Sumoylation has recently emerged as a key post-translational modification involved in many, if not all, biological processes. Small Ubiquitin-like MOdifiers (SUMOs) polypeptides are covalently attached to specific lysine residues of target proteins through a dedicated enzymatic pathway. Disruption of the SUMO enzymatic pathway in the developing brain leads to lethality indicating that this process exerts a central role during embryonic and post-natal development. However, little is still known regarding how this highly dynamic protein modification is regulated in the mammalian brain despite an increasing number of data implicating sumoylated substrates in synapse formation, synaptic communication and plasticity. The aim of this review is therefore to briefly describe the enzymatic SUMO pathway and to give an overview of our current knowledge on the function and dysfunction of protein sumoylation at the mammalian synapse.
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title_short	Sumoylation in synaptic function and dysfunction
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