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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.

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

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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