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  A MICOS-TIM22 association promotes carrier import into human mitochondria.

Callegari, S., Müller, T., Schulz, C., Lenz, C., Jans, D. C., Wissel, M., et al. (2019). A MICOS-TIM22 association promotes carrier import into human mitochondria. Journal of Molecular Biology, 431(15), 2835-2851. doi:10.1016/j.jmb.2019.05.015.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0003-A038-9 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-E3C9-A
Genre: Journal Article

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 Creators:
Callegari, S., Author
Müller, T., Author
Schulz, C., Author
Lenz, C.1, Author              
Jans, D. C.2, Author              
Wissel, M., Author
Opazo, F., Author
Rizzoli, S. O., Author
Jakobs, S.2, Author              
Urlaub, H.3, Author              
Rehling, P.4, Author              
Deckers, M., Author
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society, ou_578613              
2Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578566              
3Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              
4Max Planck Fellow Peter Rehling, ou_1298545              

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Free keywords: MICOS; Membrane insertion; Mitochondria; Mitochondrial carrier proteins; Mitochondrial import; TIM22; TIM23; Translocase
 Abstract: Mitochondrial membrane proteins with internal targeting signals are inserted into the inner membrane by the carrier translocase (TIM22 complex). For this, precursors have to be initially directed from the TOM complex in the outer mitochondrial membrane across the intermembrane space towards the TIM22 complex. How these two translocation processes are topologically coordinated is still unresolved. Using proteomic approaches, we find that the human TIM22 complex associates with the Mitochondrial Contact site and Cristae Organizing System (MICOS) complex. This association does not appear to be conserved in yeast, whereby the yeast MICOS complex instead interacts with the presequence translocase. Using a yeast mic10Δ strain and a HEK293T MIC10 knockout cell line, we characterize the role of MICOS for protein import into the mitochondrial inner membrane and matrix. We find that a physiological cristae organization promotes efficient import via the presequence pathway in yeast, while in human mitochondria, the MICOS complex is dispensable for protein import along the presequence pathway. However, in human mitochondria the MICOS complex is required for the efficient import of carrier proteins into the mitochondrial inner membrane. Our analyses suggest that in human mitochondria, positioning of the carrier translocase at the crista junction, and potentially in vicinity to the TOM complex, is required for efficient transport into the inner membrane.

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Language(s): eng - English
 Dates: 2019-05-172019-07-12
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.jmb.2019.05.015
 Degree: -

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Title: Journal of Molecular Biology
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 431 (15) Sequence Number: - Start / End Page: 2835 - 2851 Identifier: -