Lipin 2 binds phosphatidic acid by the electrostatic hydrogen bond switch mechanism independent of phosphorylation

James M. Eaton, Sankeerth Takkellapati, Robert T. Lawrence, Kelley E. McQueeney, Salome Boroda, Garrett R. Mullins, Samantha G. Sherwood, Brian N. Finck, Judit Villén, Thurl E. Harris

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

Background: Lipin 2 is a phosphatidic acid phosphatase (PAP) responsible for DAG formation at the ER membrane during lipogenesis. Results: A combination of biochemical approaches is used to characterize lipin 2 phosphatase activity and regulation. Conclusion: The electrostatic charge of PA regulates activity, but phosphorylation does not. Significance: These findings demonstrate differential regulation of PAP activity within the lipin family.

Original languageEnglish
Pages (from-to)18055-18066
Number of pages12
JournalJournal of Biological Chemistry
Volume289
Issue number26
DOIs
StatePublished - Jun 27 2014

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