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Comment
. 2018 Aug 7;115(32):E7460-E7461.
doi: 10.1073/pnas.1807968115. Epub 2018 Jul 24.

Reply to Bailey et al.: New perspectives on the novel role of the Poldip2/ACSM1 axis in a functional mammalian lipoylation salvage pathway

F Paredes  1 , B Lassègue  1 , H C Williams  1 , E A Faidley  1 , G A Benavides  2 , S M Yeligar  3   4 , K K Griendling  1 , V Darley-Usmar  2 , A San Martin  5
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Comment

Reply to Bailey et al.: New perspectives on the novel role of the Poldip2/ACSM1 axis in a functional mammalian lipoylation salvage pathway

F Paredes et al. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

The authors declare no conflict of interest.

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References

    1. Bailey PSJ, Hiltunen JK, Dieckmann CL, Kastaniotis AJ, Nathan JA. Different opinion on the reported role of Poldip2 and ACSM1 in a mammalian lipoic acid salvage pathway controlling HIF-1 activation. Proc Natl Acad Sci USA. 2018;115:E7458–E7459. - PMC - PubMed
    1. Paredes F, et al. Poldip2 is an oxygen-sensitive protein that controls PDH and αKGDH lipoylation and activation to support metabolic adaptation in hypoxia and cancer. Proc Natl Acad Sci USA. 2018;115:1789–1794. - PMC - PubMed
    1. Reed LJ, Leach FR, Koike M. Studies on a lipoic acid-activating system. J Biol Chem. 1958;232:123–142. - PubMed
    1. Fujiwara K, Okamura-Ikeda K, Motokawa Y. Purification and characterization of lipoyl-AMP:N epsilon-lysine lipoyltransferase from bovine liver mitochondria. J Biol Chem. 1994;269:16605–16609. - PubMed
    1. Fujiwara K, et al. Crystal structure of bovine lipoyltransferase in complex with lipoyl-AMP. J Mol Biol. 2007;371:222–234. - PubMed

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