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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.

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

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

Map

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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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