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Illustrating human PLD

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An Author Correction to this article was published on 31 March 2020

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Phospholipase D (PLD) regulates various cellular functions through the signaling lipid phosphatidic acid (PA). New crystal structures of human PLD1 and PLD2 reveal a catalytic mechanism, inhibitor binding, and regulation, enabling future structure-based inhibitor design and functional studies of PLD.

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Fig. 1: Structures and functions of mammalian PLD1 and PLD2.

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Acknowledgements

The authors acknowledge support from National Institutes of Health (grant # R01AR075830 to G.D.), American Heart Association (grant nos. 19TPA34910051 to G.D. and 18TPA34230046 to L.Z.), and the many scientists whose work and contributions could not be cited due to space limitations.

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, and Center for Membrane Biology, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, TX, USA

    Lei Zheng

  2. Department of Integrative Biology and Pharmacology, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, TX, USA

    Guangwei Du

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  1. Lei Zheng
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  2. Guangwei Du
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Correspondence to Guangwei Du.

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The authors declare no competing interests.

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Zheng, L., Du, G. Illustrating human PLD. Nat Chem Biol 16, 364–365 (2020). https://doi.org/10.1038/s41589-020-0503-3

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