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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.

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

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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