Crystal structure of a lipin/Pah phosphatidic acid phosphatase

Valerie I. Khayyo; Reece M. Hoffmann; Huan Wang; Justin A. Bell; John E. Burke; Karen Reue; Michael V. Airola

doi:10.1038/s41467-020-15124-z

Nature Communications (Mar 2020)

Crystal structure of a lipin/Pah phosphatidic acid phosphatase

Valerie I. Khayyo,
Reece M. Hoffmann,
Huan Wang,
Justin A. Bell,
John E. Burke,
Karen Reue,
Michael V. Airola

Affiliations

Valerie I. Khayyo: Department of Biochemistry and Cell Biology, Stony Brook University
Reece M. Hoffmann: Department of Biochemistry and Microbiology, University of Victoria
Huan Wang: Department of Human Genetics, David Geffen School of Medicine at UCLA
Justin A. Bell: Department of Biochemistry and Cell Biology, Stony Brook University
John E. Burke: Department of Biochemistry and Microbiology, University of Victoria
Karen Reue: Department of Human Genetics, David Geffen School of Medicine at UCLA
Michael V. Airola: Department of Biochemistry and Cell Biology, Stony Brook University

DOI: https://doi.org/10.1038/s41467-020-15124-z
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 11

Abstract

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Lipin/Pah phosphatidic acid phosphatases generate diacylglycerol to regulate triglyceride synthesis and cellular signaling. Here authors determine structures of Tetrahymena thermophila Pah2 and identify an N-terminal amphipathic helix essential for membrane association.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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