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ProteoNE_dynamics SIGNED

Surveillance mechanisms regulating nuclear envelope architecture and homeostasis

Total Cost €

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EC-Contrib. €

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Partnership

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 ProteoNE_dynamics project word cloud

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

sum    biotinylation    proteomics    expertise    mutations    first    elaborate    mitosis    ne    proteins    proteostasis    cells    influencing    regulation    dystrophies    describes    highlighting    lab    cell    organization    interphase    illuminate    aging    identity    contains    er    membrane    expand    myriad    depends    regulatory    rest    motility    regulates    mysterious    nuclear    inm    endoplasmic    physiological    examination    fate    combining    establishing    newly    maintaining    cellular    mammalian    muscular    continuous    view    environment    relevance    reveal    clinical    inner    syndromes    hub    confer    central    surveillance    panoramic    rates    proteome    faces    premature    eukaryotic    protein    time    underlying    reticulum    framework    living    cancer    nucleoplasm    integrity    repair    envelope    distinctive    contributions    systematic    proximity    remained    turnover    roles    aberrant    probe    diseases    functions    structure    laminopathies    gene    quality    reformation    peculiar    mechanisms    homeostasis    degradation   

Project "ProteoNE_dynamics" data sheet

The following table provides information about the project.

Coordinator
THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD 

Organization address
address: WELLINGTON SQUARE UNIVERSITY OFFICES
city: OXFORD
postcode: OX1 2JD
website: www.ox.ac.uk

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 United Kingdom [UK]
 Total cost 1˙999˙610 €
 EC max contribution 1˙999˙610 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2018-COG
 Funding Scheme ERC-COG
 Starting year 2019
 Duration (year-month-day) from 2019-07-01   to  2024-06-30

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD UK (OXFORD) coordinator 1˙999˙610.00

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 Project objective

The nuclear envelope (NE) is a major hub of eukaryotic cellular organization, influencing a myriad of processes, from gene regulation and repair to cell motility and fate. This central role of the NE depends on its elaborate structure, particularly on the organization of its inner nuclear membrane (INM). This peculiar membrane is continuous with the rest of the endoplasmic reticulum (ER) but faces the nucleoplasm and contains a distinctive set of proteins, which confer a unique identity to the INM. Importantly, mutations in several INM proteins result in a wide range of diseases, such as muscular dystrophies and premature aging syndromes, highlighting the key roles of the INM proteome in cell homeostasis. However, the mechanisms establishing and maintaining the INM proteome identity and integrity have remained mysterious. My lab recently identified a quality control system that, by targeting aberrant proteins for degradation, regulates INM identity and homeostasis. This proposal describes a framework to expand our findings and to provide a comprehensive and integrated understanding of the INM proteome. By combining my expertise in membrane protein analysis with newly developed proximity biotinylation and proteomics approaches, we will for the first time probe the complex INM environment of living mammalian cells. A systematic examination of the INM proteome, its turnover rates and changes in response to different physiological conditions will reveal functions of INM proteins and their regulatory pathways. Moreover, it will characterize INM surveillance mechanisms and evaluate their contributions to NE proteostasis. In sum, this proposal will provide a panoramic yet detailed view of the mechanisms underlying INM functions, identity and homeostasis, both in interphase and during NE reformation in mitosis. Given the clinical relevance of many INM proteins, our studies may illuminate current understanding of diseases such as laminopathies and cancer.

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