#	Pagina
attuale pagina	/open-h2020/projects/200223/index.html

Opendata, web and dolomites

ERAD_SELMA SIGNED

Mechanisms of protein translocation in ER-associated protein degradation and the related protein import into the apicoplast of Plasmodium falciparum

Total Cost €

EC-Contrib. €

Partnership

Views

Outcomes and
results

ERAD_SELMA project word cloud

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

causing import parasite translocation vitro folding site mediates degraded cells proteins intermediates serves endeavour endoplasmic cytosol thought origin energy apicoplast fundamental retro intriguing purified itself er lost plastid metabolic degradation composition combination components removal protein poorly survival mechanism intact organelles reconstitution misfolded moves moved membrane genetic falciparum endosymbiotic contain completely selma membranes cerevisiae organelle surround provided drug disease dispose reticulum experiments proteasome function parasites malaria setting outermost distinguished erad degrade symbiont conserved biochemical questions answer yeast machinery appears discard molecular

Project "ERAD_SELMA" data sheet

The following table provides information about the project.

Coordinator	MAX-PLANCK-GESELLSCHAFT ZUR FORDERUNG DER WISSENSCHAFTEN EV Organization address address: HOFGARTENSTRASSE 8 city: Munich postcode: 80539 website: www.mpg.de 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	Germany [DE]
Project website	http://www.mpibpc.mpg.de/stein
Total cost	1˙500˙000 €
EC max contribution	1˙500˙000 € (100%)
Programme	1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
Code Call	ERC-2015-STG
Funding Scheme	ERC-STG
Starting year	2016
Duration (year-month-day)	from 2016-03-01 to 2021-02-28

Partnership

Take a look of project's partnership.

#	participants	country	role	EC contrib. [€]
1	MAX-PLANCK-GESELLSCHAFT ZUR FORDERUNG DER WISSENSCHAFTEN EV MAX-PLANCK-GESELLSCHAFT ZUR FORDERUNG DER WISSENSCHAFTEN EV Organization address address: HOFGARTENSTRASSE 8 city: Munich postcode: 80539 website: www.mpg.de contact info title: n.a. name: n.a. surname: n.a. function: n.a. email: n.a. telephone: n.a. fax: n.a.	DE (Munich)	coordinator	1˙500˙000.00

Map

Project objective

The removal of misfolded proteins is an essential process in all cells. Failure to dispose of such proteins often results in disease. A particularly intriguing process serves to discard misfolded proteins from the endoplasmic reticulum (ER). The ER does not itself degrade proteins, so machinery has evolved that moves misfolded proteins into the cytosol where they can be degraded by the proteasome. This retro-translocation process is called ERAD (for ER-associated protein degradation). By comparison with other membrane translocation processes, the mechanism of ERAD is poorly understood. How are misfolded proteins distinguished from folding intermediates? How are proteins moved across the membrane? How is the energy for membrane translocation provided? To answer these fundamental questions I will use a combination of in vitro reconstitution experiments with purified proteins from S. cerevisiae and experiments in intact yeast cells. It appears that some ERAD components have been adapted to function in protein translocation in a very different setting. Many parasites like the malaria causing P. falciparum contain a plastid-like organelle, called the apicoplast. It is the site of several metabolic pathways essential for the parasite’s survival, and thus an important drug target. Like other organelles of endosymbiotic origin, the apicoplast lost most of its genetic information and has to import proteins. This is a particularly challenging endeavour because four membranes surround the apicoplast. It is thought that symbiont specific ERAD-like machinery (SELMA) mediates proteins translocation across the second-outermost membrane. However, not much is known about SELMA. What is its molecular composition? Which aspects of SELMA are conserved in comparison to the classical ERAD machinery? I will address these important questions using a completely novel combination of biochemical and genetic approaches.

Publications

List of publications.
year	authors and title	journal	last update
2020	Vedran Vasic, Niels Denkert, Claudia C. Schmidt, Dietmar Riedel, Alexander Stein, Michael Meinecke Hrd1 forms the retrotranslocation pore regulated by auto-ubiquitination and binding of misfolded proteins published pages: , ISSN: 1465-7392, DOI: 10.1038/s41556-020-0473-4	Nature Cell Biology	2020-03-05
2020	Nivedita Natarajan, Ombretta Foresti, Kim Wendrich, Alexander Stein, Pedro Carvalho Quality Control of Protein Complex Assembly by a Transmembrane Recognition Factor published pages: 108-119.e9, ISSN: 1097-2765, DOI: 10.1016/j.molcel.2019.10.003	Molecular Cell 77/1	2020-03-05
2017	Stefan Schoebel, Wei Mi, Alexander Stein, Sergey Ovchinnikov, Ryan Pavlovicz, Frank DiMaio, David Baker, Melissa G. Chambers, Huayou Su, Dongsheng Li, Tom A. Rapoport, Maofu Liao Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex with Hrd3 published pages: 352-355, ISSN: 0028-0836, DOI: 10.1038/nature23314	Nature 548/7667	2019-06-19

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