The physical state of lipid substrates provides transacylation specificity for tafazzin-Reference-Cited by-同舟云学术

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The physical state of lipid substrates provides transacylation specificity for tafazzin

Published:2012-09-02 Issue:10 Volume:8 Page:862-869
ISSN:1552-4450
Container-title:Nature Chemical Biology
language:en
Short-container-title:Nat Chem Biol

Author:

Schlame Michael,Acehan Devrim,Berno Bob,Xu Yang,Valvo Salvatore,Ren Mindong,Stokes David L,Epand Richard M

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology

Link

http://www.nature.com/articles/nchembio.1064.pdf

Reference39 articles.

1. Ma, L., Vaz, F.M., Gu, Z., Wanders, R.J.A. & Greenberg, M.L. The human TAZ gene complements mitochondrial dysfunction in the yeast taz1Δ mutant. Implications for Barth syndrome. J. Biol. Chem. 279, 44394–44399 (2004).

2. Testet, E. et al. Ypr140wp, 'the yeast tafazzin', displays a mitochondrial lysophosphatidylcholine (lyso-PC) acyltransferase activity related to triacylglycerol and mitochondrial lipid synthesis. Biochem. J. 387, 617–626 (2005).

3. Claypool, S.M., McCaffery, J.M. & Koehler, C.M. Mitochondrial mislocalization and altered assembly of a cluster of Barth syndrome mutant tafazzins. J. Cell Biol. 174, 379–390 (2006).

4. Xu, Y. et al. Characterization of tafazzin splice variants from humans and fruit flies. J. Biol. Chem. 284, 29230–29239 (2009).

5. Xu, Y., Malhotra, A., Ren, M. & Schlame, M. The enzymatic function of tafazzin. J. Biol. Chem. 281, 39217–39224 (2006).

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3. Cardiolipin remodeling maintains the inner mitochondrial membrane in cells with saturated lipidomes;2024-05-30

4. Tafazzin deficiency causes substantial remodeling in the lipidome of a mouse model of Barth Syndrome cardiomyopathy;Frontiers in Molecular Medicine;2024-04-29

5. Remodelling of mitochondrial function by import of specific lipids at multiple membrane‐contact sites;FEBS Letters;2024-02-04

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