Opendata, web and dolomites


Intramembrane chaperones : their role in folding membrane proteins

Total Cost €


EC-Contrib. €






Project "MemCHAPS" data sheet

The following table provides information about the project.


Organization address
postcode: 3584 CS

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 Netherlands [NL]
 Total cost 177˙598 €
 EC max contribution 177˙598 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2017
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2019
 Duration (year-month-day) from 2019-02-01   to  2021-05-23


Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    UNIVERSITEIT UTRECHT NL (UTRECHT) coordinator 177˙598.00


 Project objective

Membrane proteins constitute about 30 % of the eukaryotic proteome and are involved in crucial processes such as transporting molecules across membranes, mediating intracellular trafficking and functioning as signalling receptors. Most membrane proteins of varied topologies and functions are assembled in the endoplasmic reticulum (ER). While a lot is known about the protein quality control machinery in the ER, most studies have focussed on soluble lumenal proteins or domains that are accessible to the soluble ER chaperones. The complex transmembrane domains however, require assistance within the lipid bilayer. The underlying mechanism of how membrane proteins are correctly folded and assembled, remains unclear. The main goal of my project is to identify intramembrane chaperones involved in folding of membrane proteins. I plan to use ABC transporter proteins as a paradigm for multi-spanning membrane proteins with complex topologies. Using proximity-dependent biotin identification, I will screen for membrane proteins in the ER that interact with the ABC transporters. Gene silencing using CRISPR-Cas9 will demonstrate whether the interaction has a functional relevance for the stability and assembly of the ABC transporter. Building on this analysis, I plan to determine the influence of the identified chaperones by employing various biochemical techniques. My work will not only identify novel intramembrane chaperones, but will also add a spatio-temporal resolution in dissecting assisted folding of membrane proteins. A comprehensive understanding of intramembrane chaperoning will have highly relevant implications for pharmaceutical industries and will provide a basis for more selective therapeutic interventions against many membrane protein-misfolding diseases.

Are you the coordinator (or a participant) of this project? Plaese send me more information about the "MEMCHAPS" 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 ( 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 "MEMCHAPS" are provided by the European Opendata Portal: CORDIS opendata.

More projects from the same programme (H2020-EU.1.3.2.)


Emergency Decision Support System of Offshore Platform Fires

Read More  

PNAIC (2018)

Positive and Negative Asymmetry in Intergroup Contact: Its Impact on Linguistic Forms of Communication and Physiological Responses

Read More  

NaWaTL (2020)

Narrative, Writing, and the Teotihuacan Language: Exploring Language History Through Phylogenetics, Epigraphy and Iconography

Read More