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EMCOP9CRL TERMINATED

Structural basis of Cullin-RING ligase regulation by the COP9 signalosome

Total Cost €

0

EC-Contrib. €

0

Partnership

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 EMCOP9CRL project word cloud

Explore the words cloud of the EMCOP9CRL project. It provides you a very rough idea of what is the project "EMCOP9CRL" about.

sites    centred    fortunately    complexes    resolution    leads    small    proteasomal    reveal    microscopy    srs    ligase    e2    crls    sr    crl    specificity    proteins    structure    biological    substrate    degradation    receptor    protein    deneddylation    acts    subunit    holocomplexes    termed    roles    crystallization    signalosome    500kda    substrates    defects    removing    structural    relatively    pathologies    fundamental    cell    architecture    binding    plays    technological    structures    atomic    seven    complexity    shed    enzymatically    cancer    transduction    mechanistic    ubiquitin    recognition    hence    scaffold    play    inhibitory    regulation    cop9    stable    technique    homologue    cryoelectron    forming    catalytic    incompletely    prominent    ubiquitination    nedd8    stress    powerful    function    occluded    modular    progression    cycle    csn    components    near    mediated    apoptosis    e3    modulates    ring    cellular    acute    assemblies    accordingly    lt    cullin    family    mostly    core    opposite    inactivation    light    associate    multiplicity    confers    signal    lack   

Project "EMCOP9CRL" data sheet

The following table provides information about the project.

Coordinator
THE INSTITUTE OF CANCER RESEARCH: ROYAL CANCER HOSPITAL 

Organization address
address: OLD BROMPTON ROAD 123
city: LONDON
postcode: SW7 3RP
website: www.icr.ac.uk

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country United Kingdom [UK]
 Project website http://www.icr.ac.uk
 Total cost 183˙454 €
 EC max contribution 183˙454 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2014
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2015
 Duration (year-month-day) from 2015-10-12   to  2017-10-11

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    THE INSTITUTE OF CANCER RESEARCH: ROYAL CANCER HOSPITAL UK (LONDON) coordinator 183˙454.00

Map

 Project objective

The components of the Cullin-RING Ligase (CRLs) E3 ubiquitin ligase family play key roles in a wide range of cellular processes including stress response, signal transduction, apoptosis and cell cycle progression, and accordingly, defects in their function and/or regulation are prominent in many pathologies including cancer. The modular CRL architecture is centred upon one of seven different cullin scaffold proteins which associate on one side with a RING protein that acts as receptor for an E2 ligase and, on the opposite side, with a substrate receptor (SR) that confers specificity to the complex. The multiplicity of SRs allows the recognition of many different substrates by the same CRL catalytic core. CRL-mediated ubiquitination modulates the substrate´s biological activity and in many cases targets them for proteasomal degradation. The COP9 signalosome (CSN) complex plays a fundamental role in CRL regulation both by forming stable inhibitory complexes with the CRLs where the E2 ligase and substrate binding sites are occluded, and by enzymatically removing Nedd8 (a homologue of ubiquitin) from the cullin scaffold subunit, in a process termed deneddylation, that leads to inactivation of CRLs. CRL regulation by CSN is still an incompletely understood topic mostly because of the lack of high resolution CSN/CRL structures due to the challenge that the crystallization of multi-protein assemblies of such complexity represents. Fortunately, recent technological developments in another structural technique, cryoelectron microscopy, now allow structure determination of relatively small protein complexes (< 500kDa) to near-atomic resolution. Hence, we propose to use this powerful technique to reveal very high-resolution structures of several different CSN/CRL holocomplexes and shed light on the mechanistic aspects of their function.

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