ArticleThe Journal of cell biology2011
Barth syndrome mutations that cause tafazzin complex lability.
Article in The Journal of cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
- Molecular analysis of a new patient COX15 mutation provides insight into the etiology of fatal infantile cardioencephalopathy.The Journal of biological chemistry · 2026Article
- Origin and evolution of mitochondrial inner membrane composition.Journal of cell science · 2025Review
- Cardiolipin remodeling maintains the inner mitochondrial membrane in cells with saturated lipidomes.Journal of lipid research · 2024Article
- Single Cell Transcriptomic Analysis in a Mouse Model of Barth Syndrome Reveals Cell-Specific Alterations in Gene Expression and Intercellular Communication.International journal of molecular sciences · 2023Article
- A novel panel of Drosophila TAFAZZIN mutants in distinct genetic backgrounds as a resource for therapeutic testing.PloS one · 2023Article
- Barth Syndrome Cardiomyopathy: An Update.Genes · 2022Review
- Experimental models of Barth syndrome.Journal of inherited metabolic disease · 2022Review
- Cardiolipin function in the yeast S. cerevisiae and the lessons learned for Barth syndrome.Journal of inherited metabolic disease · 2022Review
- Article
- Cardiolipin Remodeling Defects Impair Mitochondrial Architecture and Function in a Murine Model of Barth Syndrome Cardiomyopathy.Circulation. Heart failure · 2021Article
- The Power of Yeast in Modelling Human Nuclear Mutations Associated with Mitochondrial Diseases.Genes · 2021Review
- Studying Lipid-Related Pathophysiology Using the Yeast Model.Frontiers in physiology · 2021Review
- The Function of Tafazzin, a Mitochondrial Phospholipid-Lysophospholipid Acyltransferase.Journal of molecular biology · 2020Review
- Phospholipid ebb and flow makes mitochondria go.The Journal of cell biology · 2020Review
- Role ofJournal of developmental biology · 2020Review
- Proteolytic Control of Lipid Metabolism.ACS chemical biology · 2019Review
- Disentangling oxidation/hydrolysis reactions of brain mitochondrial cardiolipins in pathogenesis of traumatic injury.JCI insight · 2018Article
- Cardiomyopathy-associated mutation in the ADP/ATP carrier reveals translation-dependent regulation of cytochrome c oxidase activity.Molecular biology of the cell · 2018Article
- Stendomycin selectively inhibits TIM23-dependent mitochondrial protein import.Nature chemical biology · 2017Article
- Metalloproteases of the Inner Mitochondrial Membrane.Biochemistry · 2017Review
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Authors and funding
5 authors.
Funding
Abstract
Deficits in mitochondrial function result in many human diseases. The X-linked disease Barth syndrome (BTHS) is caused by mutations in the tafazzin gene TAZ1. Its product, Taz1p, participates in the metabolism of cardiolipin, the signature phospholipid of mitochondria. In this paper, a yeast BTHS mutant tafazzin panel is established, and 18 of the 21 tested BTHS missense mutations cannot functionally replace endogenous tafazzin. Four BTHS mutant tafazzins expressed at low levels are degraded by the intermembrane space AAA (i-AAA) protease, suggesting misfolding of the mutant polypeptides. Paradoxically, each of these mutant tafazzins assembles in normal protein complexes. Furthermore, in the absence of the i-AAA protease, increased expression and assembly of two of the BTHS mutants improve their function. However, the BTHS mutant complexes are extremely unstable and accumulate as insoluble aggregates when disassembled in the absence of the i-AAA protease. Thus, the loss of function for these BTHS mutants results from the inherent instability of the mutant tafazzin complexes.
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