The mitochondrial inner membrane protein LETM1 modulates cristae organization through its LETM domain.

Autor: Nakamura S; Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka, 812-8582, Japan., Matsui A; Department of Life Science, Rikkyo University, Tokyo, 171-8501, Japan., Akabane S; Department of Life Science, Rikkyo University, Tokyo, 171-8501, Japan., Tamura Y; Department of Material and Biological Chemistry, Faculty of Science, Yamagata University, Yamagata, 990-8560, Japan., Hatano A; Department of Life Science, Rikkyo University, Tokyo, 171-8501, Japan., Miyano Y; Department of Life Science, Rikkyo University, Tokyo, 171-8501, Japan., Omote H; Department of Membrane Biochemistry, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama, 700-8530, Japan., Kajikawa M; Laboratory for Infectious Immunity, RIKEN Research Center for Allergy and Immunology, Kanagawa, 230-0045, Japan., Maenaka K; Laboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, 060-0812, Japan., Moriyama Y; Department of Membrane Biochemistry, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama, 700-8530, Japan., Endo T; Faculty of Life Sciences, Kyoto Sangyo University, Kyoto, 603-8555, Japan., Oka T; Department of Life Science, Rikkyo University, Tokyo, 171-8501, Japan. toka@rikkyo.ac.jp.
Jazyk: angličtina
Zdroj: Communications biology [Commun Biol] 2020 Mar 05; Vol. 3 (1), pp. 99. Date of Electronic Publication: 2020 Mar 05.
DOI: 10.1038/s42003-020-0832-5
Abstrakt: LETM1 is a mitochondrial inner membrane protein that is required for maintaining the mitochondrial morphology and cristae structures, and regulates mitochondrial ion homeostasis. Here we report a role of LETM1 in the organization of cristae structures. We identified four amino acid residues of human LETM1 that are crucial for complementation of the growth deficiency caused by gene deletion of a yeast LETM1 orthologue. Substituting amino acid residues with alanine disrupts the correct assembly of a protein complex containing LETM1 and prevents changes in the mitochondrial morphology induced by exogenous LETM1 expression. Moreover, the LETM1 protein changes the shapes of the membranes of in vitro-reconstituted proteoliposomes, leading to the formation of invaginated membrane structures on artificial liposomes. LETM1 mutant proteins with alanine substitutions fail to facilitate the formation of invaginated membrane structures, suggesting that LETM1 plays a fundamental role in the organization of mitochondrial membrane morphology.
Databáze: MEDLINE
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