Opendata, web and dolomites

ProteoNE_dynamics SIGNED

Surveillance mechanisms regulating nuclear envelope architecture and homeostasis

Total Cost €

0

EC-Contrib. €

0

Partnership

0

Views

0

 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.

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

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

Map

 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.

Are you the coordinator (or a participant) of this project? Plaese send me more information about the "PROTEONE_DYNAMICS" project.

For instance: the website url (it has not provided by EU-opendata yet), the logo, a more detailed description of the project (in plain text as a rtf file or a word file), some pictures (as picture files, not embedded into any word file), twitter account, linkedin page, etc.

Send me an  email (fabio@fabiodisconzi.com) and I put them in your project's page as son as possible.

Thanks. And then put a link of this page into your project's website.

The information about "PROTEONE_DYNAMICS" are provided by the European Opendata Portal: CORDIS opendata.

More projects from the same programme (H2020-EU.1.1.)

CohoSing (2019)

Cohomology and Singularities

Read More  

AST (2019)

Automatic System Testing

Read More  

QLite (2019)

Quantum Light Enterprise

Read More