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Peer-Reviewed Publication
Cell Rep2026;45(8):117857.August 14, 2026Journal Article

Succinate and its carrier Sfc1 mediate metabolic control of mitochondrial protein import by the TIM23 translocase.

Koyeli Das1, Rituparna Samanta2, Tamar Ziv3, Johannes M Herrmann4, Bella Kalderon1, Ophry Pines5
1Department of Microbiology and Molecular Genetics, The Institute for Medical Research Israel-Canada (IMRIC), Faculty of Medicine, The Hebrew University of Jerusalem, P.O.B 12272, Jerusalem 91120, Israel.
2Department of Chemical, Biological and Materials Engineering, University of South Florida, Tampa, FL 33620, USA.
3The Smoler Proteomics Center, Technion Israel Institute of Technology, Haifa, Israel.
4Cell Biology, University of Kaiserslautern, RPTU, Erwin-Schrödinger-Strasse 13, 67663 Kaiserslautern, Germany.
5Department of Microbiology and Molecular Genetics, The Institute for Medical Research Israel-Canada (IMRIC), Faculty of Medicine, The Hebrew University of Jerusalem, P.O.B 12272, Jerusalem 91120, Israel. Electronic address: ophryp@ekmd.huji.ac.il.

Abstract

Tim23 is an essential component of the mitochondrial inner membrane translocase and Sfc1 is a carrier that exchanges succinate for fumarate across that membrane. Sfc1 and succinic acid availability regulate dual targeting of fumarase and aconitase by facilitating mitochondrial import of their newly synthesized precursors, as shown by pulse-chase experiments. Here, we show that Sfc1 associates with…

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