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PMID:17420445

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Citation

Kim, Y, Gentry, MS, Harris, TE, Wiley, SE, Lawrence, JC Jr and Dixon, JE (2007) A conserved phosphatase cascade that regulates nuclear membrane biogenesis. Proc. Natl. Acad. Sci. U.S.A. 104:6596-601

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 nem1Delta 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.

Links

PubMed PMC1871831 Online version:10.1073/pnas.0702099104

Keywords

Amino Acid Sequence; Animals; COS Cells; Cell Line; Cercopithecus aethiops; Conserved Sequence; Cricetinae; Drosophila Proteins/chemistry; Drosophila Proteins/physiology; Drosophila melanogaster/enzymology; Drosophila melanogaster/metabolism; HeLa Cells; Humans; Molecular Sequence Data; Nerve Tissue Proteins/chemistry; Nerve Tissue Proteins/physiology; Nuclear Envelope/enzymology; Nuclear Envelope/metabolism; Nuclear Proteins/chemistry; Nuclear Proteins/physiology; Phosphoprotein Phosphatases/chemistry; Phosphoprotein Phosphatases/physiology; Saccharomyces cerevisiae/enzymology; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae Proteins/chemistry; Saccharomyces cerevisiae Proteins/physiology; Signal Transduction/physiology

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:CNEP1

located_in

GO:0005789: endoplasmic reticulum membrane

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

HUMAN:CNEP1

located_in

GO:0005635: nuclear envelope

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

HUMAN:CNEP1

part_of

GO:0005789: endoplasmic reticulum membrane

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

HUMAN:CNEP1

involved_in

GO:0006470: protein dephosphorylation

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:CNEP1

involved_in

GO:0006998: nuclear envelope organization

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:CNEP1

part_of

GO:0005635: nuclear envelope

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

HUMAN:CNEP1

enables

GO:0004722: protein serine/threonine phosphatase activity

ECO:0000315: mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete


See also

References

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