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.

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

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.)

ENUF (2019)

Evaluation of Novel Ultra-Fast selective III-V Epitaxy

Read More  

Aware (2019)

Aiding Antibiotic Development with Deep Analysis of Resistance Evolution

Read More  

E-DURA (2018)

Commercialization of novel soft neural interfaces

Read More