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Riemer lab - Institute for Biochemistry

CONTROL OF DUAL LOCALIZATION BETWEEN CYTOSOL AND MITOCHONDRIAL IMS

Mitochondria are highly dynamic organelles with critical importance for the cell. To fulfill their various functions and to adjust to different cellular demands, their proteome needs to be highly plastic with respect to its quantity (amounts, activity) and quality (different proteins). This requires a dynamic regulation of mitochondrial biogenesis, protein import, and protein homeostasis on different levels. In this project, we will investigate a novel mechanism that controls dual localization of mitochondrial proteins. Here, cytosolic processing of protein N-termini renders specific precursor proteins susceptible to proteasomal degradation, ensuring that they are only present in mitochondria. On the other hand, preventing this processing sustains a functional non-mitochondrial protein pool.

Konstantin Weiß

PhD student since August 2020

EMail: konstantin.weiss[at]uni-koeln.de

"I obtained my Bachelor’s and Master’s degree in Biochemistry at the Goethe University Frankfurt/Main. During my studies I could gain insights into different fields of research ranging from protein localization studies to drug discovery in lung cancer and structural biology. Now I am working in the Riemer lab where I employ cell biological and protein biochemical methods to investigate the role of a cytosolic protease in dual protein localization and the underlying regulatory mechanisms."

Publications

  • Dipeptidyl peptidase 9 triggers BRCA2 degradation and promotes DNA damage repair. Bolgi O, Silva-Garcia M, Ross B, Pilla E, Kari V, Killisch M, Spitzner M, Stark N, Lenz C, Weiss K, Donzelli L, Gorrell MD, Grade M, Riemer J, Urlaub H, Dobbelstein M, Huber R, Geiss-Friedlander R. EMBO Rep. 2022 Aug 1:e54136. doi: 10.15252/embr.202154136. Online ahead of print. PMID: 35912982

Sarah Gerlich

PhD student since December 2020

Gender & Diversity Board Member

EMail: sgerlich[at]smail.uni-koeln.de

"I studied biochemistry at the university of Cologne and focussed during my Master studies on mitochondrial and medical biochemistry. Currently, I am working on my PhD project about cellular adaptation processes to oxidative stress in the working group of Jan Riemer."

Publications

  • AIFM1 is a component of the mitochondrial disulfide relay that drives complex I assembly through efficient import of NDUFS5. Salscheider SL, Gerlich S, Cabrera-Orefice A, Peker E, Rothemann RA, Murschall LM, Finger Y, Szczepanowska K, Ahmadi ZA, Guerrero-Castillo S, Erdogan A, Becker M, Ali M, Habich M, Petrungaro C, Burdina N, Schwarz G, Klußmann M, Neundorf I, Stroud DA, Ryan MT, Trifunovic A, Brandt U, Riemer J. EMBO J. 2022 Jul 20:e110784. doi: 10.15252/embj.2022110784. Online ahead of print. PMID: 35859387

  • Proteasomal degradation induced by DPP9-mediated processing competes with mitochondrial protein import. Finger Y, Habich M, Gerlich S, Urbanczyk S, van de Logt E, Koch J, Schu L, Lapacz KJ, Ali M, Petrungaro C, Salscheider SL, Pichlo C, Baumann U, Mielenz D, Dengjel J, Brachvogel B, Hofmann K, Riemer J. EMBO J. 2020 Oct 1;39(19):e103889. doi: 10.15252/embj.2019103889. Epub 2020 Aug 20. PMID: 32815200

Esra Peker

PhD student since June 2018

EMail: epeker[at]smail.uni-koeln.de

"I obtained my Bachelor´s and Master´s degree in Chemistry at the University of Cologne. During my studies I focused on biochemistry and had the opportunity to stay in the Riemer lab for my PhD. I am working on a subgroup of small proteins that follow an unconventional import pathway into mitochondria."

Publications

  • AIFM1 is a component of the mitochondrial disulfide relay that drives complex I assembly through efficient import of NDUFS5. Salscheider SL, Gerlich S, Cabrera-Orefice A, Peker E, Rothemann RA, Murschall LM, Finger Y, Szczepanowska K, Ahmadi ZA, Guerrero-Castillo S, Erdogan A, Becker M, Ali M, Habich M, Petrungaro C, Burdina N, Schwarz G, Klußmann M, Neundorf I, Stroud DA, Ryan MT, Trifunovic A, Brandt U, Riemer J. EMBO J. 2022 Jul 20:e110784. doi: 10.15252/embj.2022110784. Online ahead of print. PMID: 35859387

  • Mitochondria shed their outer membrane in response to infection-induced stress. Li X, Straub J, Medeiros TC, Mehra C, den Brave F, Peker E, Atanassov I, Stillger K, Michaelis JB, Burbridge E, Adrain C, Münch C, Riemer J, Becker T, Pernas LF. Science. 2022 Jan 14;375(6577):eabi4343. doi: 10.1126/science.abi4343. Epub 2022 Jan 14. PMID: 35025629

  • Erv1 and Cytochrome c Mediate Rapid Electron Transfer via A Collision-Type Interaction. Peker E, Erdogan AJ, Volkov AN, Riemer J. J Mol Biol. 2021 Jul 23;433(15):167045. doi: 10.1016/j.jmb.2021.167045. Epub 2021 May 8. PMID: 33971209

  • The C-terminal region of the oxidoreductase MIA40 stabilizes its cytosolic precursor during mitochondrial import. Murschall LM, Gerhards A, MacVicar T, Peker E, Hasberg L, Wawra S, Langer T, Riemer J. BMC Biol. 2020 Aug 6;18(1):96. doi: 10.1186/s12915-020-00824-1. PMID: 32762682

  • Protein Import Assay into Mitochondria Isolated from Human Cells. Murschall LM, Peker E, MacVicar T, Langer T, Riemer J. Bio Protoc. 2021 Jun 20;11(12):e4057. doi: 10.21769/BioProtoc.4057. eCollection 2021 Jun 20. PMID: 34263000