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Nedd8Activate SIGNED

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

Total Cost €

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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.

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

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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