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AIFM1 is a component of the mitochondrial disulfide relay that drives complex I assembly through efficient import of NDUFS5

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AIFM1 is a component of the mitochondrial disulfide relay that drives complex I assembly through efficient import of NDUFS5. / Salscheider, Silja Lucia; Gerlich, Sarah; Cabrera-Orefice, Alfredo; Peker, Esra; Rothemann, Robin Alexander; Murschall, Lena Maria; Finger, Yannik; Szczepanowska, Karolina; Ahmadi, Zeinab Alsadat; Guerrero-Castillo, Sergio; Erdogan, Alican; Becker, Mark; Ali, Muna; Habich, Markus; Petrungaro, Carmelina; Burdina, Nele; Schwarz, Guenter; Klußmann, Merlin; Neundorf, Ines; Stroud, David A; Ryan, Michael T; Trifunovic, Aleksandra; Brandt, Ulrich; Riemer, Jan.

in: EMBO J, Jahrgang 41, Nr. 17, 01.09.2022, S. e110784.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

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 2022, 'AIFM1 is a component of the mitochondrial disulfide relay that drives complex I assembly through efficient import of NDUFS5', EMBO J, Jg. 41, Nr. 17, S. e110784. https://doi.org/10.15252/embj.2022110784

APA

Salscheider, S. L., Gerlich, S., Cabrera-Orefice, A., Peker, E., Rothemann, R. A., Murschall, L. M., Finger, Y., Szczepanowska, K., Ahmadi, Z. A., Guerrero-Castillo, S., Erdogan, A., Becker, M., Ali, M., Habich, M., Petrungaro, C., Burdina, N., Schwarz, G., Klußmann, M., Neundorf, I., ... Riemer, J. (2022). AIFM1 is a component of the mitochondrial disulfide relay that drives complex I assembly through efficient import of NDUFS5. EMBO J, 41(17), e110784. https://doi.org/10.15252/embj.2022110784

Vancouver

Salscheider SL, Gerlich S, Cabrera-Orefice A, Peker E, Rothemann RA, Murschall LM et al. AIFM1 is a component of the mitochondrial disulfide relay that drives complex I assembly through efficient import of NDUFS5. EMBO J. 2022 Sep 1;41(17):e110784. https://doi.org/10.15252/embj.2022110784

Bibtex

@article{331b0d0f75584678aeee1e300a46f054,
title = "AIFM1 is a component of the mitochondrial disulfide relay that drives complex I assembly through efficient import of NDUFS5",
abstract = "The mitochondrial intermembrane space protein AIFM1 has been reported to mediate the import of MIA40/CHCHD4, which forms the import receptor in the mitochondrial disulfide relay. Here, we demonstrate that AIFM1 and MIA40/CHCHD4 cooperate beyond this MIA40/CHCHD4 import. We show that AIFM1 and MIA40/CHCHD4 form a stable long-lived complex in vitro, in different cell lines, and in tissues. In HEK293 cells lacking AIFM1, levels of MIA40 are unchanged, but the protein is present in the monomeric form. Monomeric MIA40 neither efficiently interacts with nor mediates the import of specific substrates. The import defect is especially severe for NDUFS5, a subunit of complex I of the respiratory chain. As a consequence, NDUFS5 accumulates in the cytosol and undergoes rapid proteasomal degradation. Lack of mitochondrial NDUFS5 in turn results in stalling of complex I assembly. Collectively, we demonstrate that AIFM1 serves two overlapping functions: importing MIA40/CHCHD4 and constituting an integral part of the disulfide relay that ensures efficient interaction of MIA40/CHCHD4 with specific substrates.",
keywords = "Apoptosis Inducing Factor/metabolism, Disulfides/metabolism, Electron Transport Complex I/metabolism, HEK293 Cells, Humans, Mitochondrial Membrane Transport Proteins/genetics, Mitochondrial Precursor Protein Import Complex Proteins, Mitochondrial Proteins/genetics, Oxidation-Reduction, Protein Transport",
author = "Salscheider, {Silja Lucia} and Sarah Gerlich and Alfredo Cabrera-Orefice and Esra Peker and Rothemann, {Robin Alexander} and Murschall, {Lena Maria} and Yannik Finger and Karolina Szczepanowska and Ahmadi, {Zeinab Alsadat} and Sergio Guerrero-Castillo and Alican Erdogan and Mark Becker and Muna Ali and Markus Habich and Carmelina Petrungaro and Nele Burdina and Guenter Schwarz and Merlin Klu{\ss}mann and Ines Neundorf and Stroud, {David A} and Ryan, {Michael T} and Aleksandra Trifunovic and Ulrich Brandt and Jan Riemer",
note = "{\textcopyright} 2022 The Authors. Published under the terms of the CC BY NC ND 4.0 license.",
year = "2022",
month = sep,
day = "1",
doi = "10.15252/embj.2022110784",
language = "English",
volume = "41",
pages = "e110784",
journal = "EMBO J",
issn = "0261-4189",
publisher = "NATURE PUBLISHING GROUP",
number = "17",

}

RIS

TY - JOUR

T1 - AIFM1 is a component of the mitochondrial disulfide relay that drives complex I assembly through efficient import of NDUFS5

AU - Salscheider, Silja Lucia

AU - Gerlich, Sarah

AU - Cabrera-Orefice, Alfredo

AU - Peker, Esra

AU - Rothemann, Robin Alexander

AU - Murschall, Lena Maria

AU - Finger, Yannik

AU - Szczepanowska, Karolina

AU - Ahmadi, Zeinab Alsadat

AU - Guerrero-Castillo, Sergio

AU - Erdogan, Alican

AU - Becker, Mark

AU - Ali, Muna

AU - Habich, Markus

AU - Petrungaro, Carmelina

AU - Burdina, Nele

AU - Schwarz, Guenter

AU - Klußmann, Merlin

AU - Neundorf, Ines

AU - Stroud, David A

AU - Ryan, Michael T

AU - Trifunovic, Aleksandra

AU - Brandt, Ulrich

AU - Riemer, Jan

N1 - © 2022 The Authors. Published under the terms of the CC BY NC ND 4.0 license.

PY - 2022/9/1

Y1 - 2022/9/1

N2 - The mitochondrial intermembrane space protein AIFM1 has been reported to mediate the import of MIA40/CHCHD4, which forms the import receptor in the mitochondrial disulfide relay. Here, we demonstrate that AIFM1 and MIA40/CHCHD4 cooperate beyond this MIA40/CHCHD4 import. We show that AIFM1 and MIA40/CHCHD4 form a stable long-lived complex in vitro, in different cell lines, and in tissues. In HEK293 cells lacking AIFM1, levels of MIA40 are unchanged, but the protein is present in the monomeric form. Monomeric MIA40 neither efficiently interacts with nor mediates the import of specific substrates. The import defect is especially severe for NDUFS5, a subunit of complex I of the respiratory chain. As a consequence, NDUFS5 accumulates in the cytosol and undergoes rapid proteasomal degradation. Lack of mitochondrial NDUFS5 in turn results in stalling of complex I assembly. Collectively, we demonstrate that AIFM1 serves two overlapping functions: importing MIA40/CHCHD4 and constituting an integral part of the disulfide relay that ensures efficient interaction of MIA40/CHCHD4 with specific substrates.

AB - The mitochondrial intermembrane space protein AIFM1 has been reported to mediate the import of MIA40/CHCHD4, which forms the import receptor in the mitochondrial disulfide relay. Here, we demonstrate that AIFM1 and MIA40/CHCHD4 cooperate beyond this MIA40/CHCHD4 import. We show that AIFM1 and MIA40/CHCHD4 form a stable long-lived complex in vitro, in different cell lines, and in tissues. In HEK293 cells lacking AIFM1, levels of MIA40 are unchanged, but the protein is present in the monomeric form. Monomeric MIA40 neither efficiently interacts with nor mediates the import of specific substrates. The import defect is especially severe for NDUFS5, a subunit of complex I of the respiratory chain. As a consequence, NDUFS5 accumulates in the cytosol and undergoes rapid proteasomal degradation. Lack of mitochondrial NDUFS5 in turn results in stalling of complex I assembly. Collectively, we demonstrate that AIFM1 serves two overlapping functions: importing MIA40/CHCHD4 and constituting an integral part of the disulfide relay that ensures efficient interaction of MIA40/CHCHD4 with specific substrates.

KW - Apoptosis Inducing Factor/metabolism

KW - Disulfides/metabolism

KW - Electron Transport Complex I/metabolism

KW - HEK293 Cells

KW - Humans

KW - Mitochondrial Membrane Transport Proteins/genetics

KW - Mitochondrial Precursor Protein Import Complex Proteins

KW - Mitochondrial Proteins/genetics

KW - Oxidation-Reduction

KW - Protein Transport

U2 - 10.15252/embj.2022110784

DO - 10.15252/embj.2022110784

M3 - SCORING: Journal article

C2 - 35859387

VL - 41

SP - e110784

JO - EMBO J

JF - EMBO J

SN - 0261-4189

IS - 17

ER -