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Nedd8Activate SIGNED

How does the ubiquitin-like protein NEDD8 activate ubiquitin ligase machineries?

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EC-Contrib. €

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Partnership

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 Nedd8Activate project word cloud

Explore the words cloud of the Nedd8Activate project. It provides you a very rough idea of what is the project "Nedd8Activate" about.

discover    form    interacting    ubiquitin    affinity    ring    reagents    biochemical    cells    modification    ligases    biological    rbr    nedd8    activated    action    cullin    elusive    generate    devise    structures    chemical    discovered    activates    mediate    families    ariadne    cell    nearly    temporally    domains    regulate    mechanism    functions    resource    family    em    enzymes    neddylated    atypical    ubls    visualize    nonetheless    translational    multiple    disease    e3    regulates    act    chains    half    class    polyubiquitin    tour    cryo    identical    transform    monoubiquitylation    interactions    eukaryotic    fraction    paradigms    e3s    ubiquitins    molecular    crls    comprehensively    ligase    first    capture    tools    ubiquitylating    biology    regulation    purify    label    goals    track    ubl    giant    post    assemblies    fleeting    structural    mark    de    activating    little    forms    monoubiquitin    reactions    substrates    peculiar    proteins    modifications    subunits    mechanisms    58    detect    regulatory    force   

Project "Nedd8Activate" data sheet

The following table provides information about the project.

Coordinator
MAX-PLANCK-GESELLSCHAFT ZUR FORDERUNG DER WISSENSCHAFTEN EV 

Organization address
address: HOFGARTENSTRASSE 8
city: Munich
postcode: 80539
website: www.mpg.de

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 Germany [DE]
 Total cost 2˙193˙871 €
 EC max contribution 2˙193˙871 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2017-ADG
 Funding Scheme ERC-ADG
 Starting year 2018
 Duration (year-month-day) from 2018-10-01   to  2023-09-30

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    MAX-PLANCK-GESELLSCHAFT ZUR FORDERUNG DER WISSENSCHAFTEN EV DE (Munich) coordinator 2˙193˙871.00

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 Project objective

Post-translational modification by ubiquitin and ubiquitin-like proteins (UBLs) is a major eukaryotic regulatory mechanism. Nonetheless, we have little understanding of the detailed mechanisms by which most E3 ligases mark specific targets with monoubiquitin, multiple ubiquitins or specific polyubiquitin chains, or of how UBL modifications transform the functions of their targets. This proposal addresses both problems. First, we will discover the structural mechanisms by which the UBL NEDD8 (58% identical to ubiquitin) activates numerous distinct functions of its targets, which are cullin subunits of cullin-RING E3 ubiquitin ligases (CRLs). Second, we will take a tour-de-force structural, biochemical, and molecular cell biological approach to determine how NEDD8-activated E3 ligases regulate their substrates. Because CRLs form nearly half of all E3 ligases, and as we recently discovered, neddylated CRLs act in part by activating monoubiquitylation by another family of E3 ligases (Ariadne-family RBR E3s), the proposed studies will establish paradigms for a major fraction of ubiquitylating enzymes. To achieve these goals, we will devise novel chemical biology tools to capture fleeting assemblies that typically only occur during chemical reactions, and visualize structures of neddylated CRLs “in action” by cryo EM. We will generate a resource of novel reagents that detect, label, and affinity purify activated forms of E3 ligases to temporally track their interactions during pathways they regulate in cells. And we will define the mechanisms and structures of a class of atypical, disease-associated giant E3 ligases whose domains and interacting partners are so peculiar that their activities remain elusive. Overall, we will comprehensively define how a UBL directly regulates its targets, and how two major E3 ligase families mediate regulation.

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