A conserved phosphatase cascade that regulates nuclear membrane biogenesis

Youngjun Kim, Matthew S. Gentry, Thurl E. Harris, Sandra E. Wiley, John C. Lawrence, Jack E. Dixon

Research output: Contribution to journalArticlepeer-review

114 Scopus citations

Abstract

A newly emerging family of phosphatases that are members of the haloacid dehalogenase superfamily contains the catalytic motif DXDX(T/V). A member of this DXDX(T/V) phosphatase family known as Dullard was recently shown to be a potential regulator of neural tube development in Xenopus [Satow R, Chan TC, Asashima M (2002) Biochem Biophys Res Commun 295:85-91]. Herein, we demonstrate that human Dullard and the yeast protein Nem1p perform similar functions in mammalian cells and yeast cells, respectively. In addition to similarity in primary sequence. Dullard and Nem1p possess similar domains and show similar substrate preferences, and both localize to the nuclear envelope. Additionally, we show that human Dullard can rescue the aberrant nuclear envelope morphology of nem1Δ yeast cells, functionally replacing Nem1p. Finally, Nem1p, has been shown to deposphorylate the yeast phosphatidic acid phosphatase Smp2p [Santos-Rosa H, Leung J, Grimsey N, Peak-Chew S, Siniossoglou S (2005) EMBO J 24:1931-1941], and we show that Dullard dephosphorylates the mammalian phospatidic acid phosphatase, lipin. Therefore, we propose that Dullard participates in a unique phosphatase cascade regulating nuclear membrane biogenesis, and that this cascade is conserved from yeast to mammals.

Original languageEnglish
Pages (from-to)6596-6601
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume104
Issue number16
DOIs
StatePublished - Apr 17 2007

Keywords

  • C-terminal domain phosphatase
  • Dullard
  • Lipin
  • Nuclear envelope biogenesis
  • Phosphatidic acid phosphatase

ASJC Scopus subject areas

  • General

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