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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.

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

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

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 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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