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NMR-DisAgg SIGNED

The Dynamic Composition of the Protein Chaperone Network: Unraveling Human Protein Disaggregation via NMR Spectroscopy

Total Cost €

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EC-Contrib. €

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Partnership

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 NMR-DisAgg project word cloud

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

ultimately    refolding    toxic    ideally    performed    group    lab    substrate    structural    protect    recognition    responsible    schemes    disease    molecular    regarding    dnaj    hsp40    combinations    host    potentially    nmr    complexes    nature    remodeling    functions    structure    diverse    heat    methyl    dynamic    cellular    break    certain    shock    performing    little    combining    amyloids    assays    chaperone    protein    hsp70    reaction    aside    operate    client    observe    diseases    characterization    transient    cpmg    populated    perform    biophysical    proven    recognizing    shsp    cells    techniques    functional    exact    itself    proteins    extremely    human    aggregates    small    experiments    trosy    suited    series    initial    clients    additional    discovered    maintaining    dissolving    time    fibers    first    monitor    homeostasis    though    types    interactions    disaggregation    amyloid    linked    apart    cest    families    course    members    chaperones    critical    labeling    neurodegenerative   

Project "NMR-DisAgg" data sheet

The following table provides information about the project.

Coordinator
WEIZMANN INSTITUTE OF SCIENCE 

Organization address
address: HERZL STREET 234
city: REHOVOT
postcode: 7610001
website: www.weizmann.ac.il

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 Israel [IL]
 Total cost 1˙499˙956 €
 EC max contribution 1˙499˙956 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2018-STG
 Funding Scheme ERC-STG
 Starting year 2018
 Duration (year-month-day) from 2018-09-01   to  2023-08-31

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    WEIZMANN INSTITUTE OF SCIENCE IL (REHOVOT) coordinator 1˙499˙956.00

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 Project objective

Molecular chaperones are a diverse group of proteins critical to maintaining cellular homeostasis. Aside from protein refolding, it has recently been discovered that certain combinations of human chaperones can break apart toxic protein aggregates and even amyloids that have been linked to a host of neurodegenerative diseases. The first chaperones in this disaggregation reaction that are responsible for recognizing and performing initial remodeling of aggregates, are members of the Hsp40 (DnaJ) and small heat shock protein (sHSP) families. Very little, though, is known regarding how these chaperones perform their functions, and characterization of sHsp- and DnaJ-substrate complexes by most structural techniques has proven extremely challenging, as most chaperones are dynamic in nature and typically operate through a series of transient interactions with both their clients and other chaperones. The advanced NMR techniques used in our lab, however, are ideally suited for the study of these exact types of dynamic systems, and include recently developed experiments (CEST, CPMG) that allow us to monitor the transient and low populated protein states typical of chaperone-chaperone and chaperone-client interactions, as well as to study the structure of these potentially very large protein complexes (methyl-TROSY). By exploiting these NMR methodologies and additional, novel labeling schemes, we will characterize, for the first time, the recognition and substrate remodeling performed by the many members of the DnaJ and sHsp chaperone families on their clients. We will then take these approaches one step further and develop real time NMR experiments to observe the client remodeling performed over the course of the disaggregation reaction itself. By combining advanced NMR with biophysical and functional assays, we ultimately aim to identify the specific sets of chaperones that, with the Hsp70 system, protect our cells by dissolving disease-linked aggregates and amyloid fibers.

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