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ERAD_SELMA SIGNED

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

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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 DE (Munich) coordinator 1˙500˙000.00

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 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

year authors and title journal last update
List of publications.
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

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