SUMOKAINATE

SUMOylation and kainate receptor synaptic plasticity

 Coordinatore UNIVERSITY OF BRISTOL 

 Organization address address: TYNDALL AVENUE SENATE HOUSE
city: BRISTOL
postcode: BS8 1TH

contact info
Titolo: Ms.
Nome: Johanna
Cognome: Rule
Email: send email
Telefono: -9288769
Fax: -9250973

 Nazionalità Coordinatore United Kingdom [UK]
 Totale costo 0 €
 EC contributo 172˙434 €
 Programma FP7-PEOPLE
Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
 Code Call FP7-PEOPLE-IEF-2008
 Funding Scheme MC-IEF
 Anno di inizio 2009
 Periodo (anno-mese-giorno) 2009-04-01   -   2011-03-31

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    UNIVERSITY OF BRISTOL

 Organization address address: TYNDALL AVENUE SENATE HOUSE
city: BRISTOL
postcode: BS8 1TH

contact info
Titolo: Ms.
Nome: Johanna
Cognome: Rule
Email: send email
Telefono: -9288769
Fax: -9250973

UK (BRISTOL) coordinator 172˙434.64

Mappa


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kars    dependent    kar    plasticity    synaptic    mechanism    sumo    proteins    sumoylation    pdz    protein    glur    techniques   

 Obiettivo del progetto (Objective)

'The aim of this work is to demonstrate the role of SUMO (Small Ubiquitin like MOdifier) in synaptic plasticity. Specifically, my goal is to show that synaptic kainate receptors (KARs) are regulated in an activity-dependent manner that involves their SUMOylation. Recently, Mellor and Henley have discovered that the KAR subunit GluR6 is a substrate for SUMO and that SUMOylation of GluR6 causes KARs to be endocytosed. This was demonstrated for synaptic KARs at mossy fibre synapses in the hippocampus, suggesting that it is a mechanism for activity-dependent regulation of KARs at this synapse. In the post-synaptic density, PDZ-domain-containing proteins play a prominent role in organizing synaptic elements. My hypothesis is that SUMOylation of GluR6 influences the interaction of KARs with PDZ binding proteins, thus leading to KAR plasticity. In addition, phosphorylation of GluR6 by protein kinase C (PKC) could potentially regulate SUMOylation itself. To test these hypotheses, I intend to employ electrophysiological techniques (patch-clamp recording) in acute and cultured thalamocortical and hippocampal slices, combining them with biochemical techniques to block specific protein-protein interactions and modulate the level of GluR6 SUMOylation. Since the role of SUMOylation is largely unknown outside of the nucleus, its involvement in synaptic plasticity constitutes a major new function for SUMO. Therefore, SUMOylation provides a novel and intriguing mechanism underlying synaptic plasticity.'

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