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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.

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

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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