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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.

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

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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