Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family

Scott M. Hammond; Yelena M. Altshuller; Tsung Chang Sung; Simon A. Rudge; Kristine Rose; Jo Anne Engebrecht; Andrew J. Morris; Michael A. Frohman

doi:10.1074/jbc.270.50.29640

Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family

Scott M. Hammond
, Yelena M. Altshuller
, Tsung Chang Sung
, Simon A. Rudge
, Kristine Rose
, Jo Anne Engebrecht
, Andrew J. Morris
, Michael A. Frohman

Internal Medicine

Producción científica: Article › revisión exhaustiva

624 Citas (Scopus)

Resumen

Activation of phosphatidylcholine-specific phospholipase D (PLD) has been implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. We report here the identification of the first human PLD cDNA, which defines a new and highly conserved gene family. Characterization of recombinant human PLD1 reveals that it is membrane-associated, selective for phosphatidylcholine, stimulated by phosphatidylinositol 4,5-bisphosphate, activated by the monomeric G-protein ADP-ribosylation factor-1, and inhibited by oleate. PLD1 likely encodes the gene product responsible for the most widely studied endogenous PLD activity.

Idioma original	English
Páginas (desde-hasta)	29640-29643
Número de páginas	4
Publicación	Journal of Biological Chemistry
Volumen	270
N.º	50
DOI	https://doi.org/10.1074/jbc.270.50.29640
Estado	Published - dic 15 1995

Nota bibliográfica

Funding Information:
Accepted Januaty 9. 1992. From the Department ofPsychiatry, University ofPittsburgh School of Medicine, and the Western Psychiatric Institute and Clinic, Pittsburgh, PA. Preparation of this article was supported in part by NIMH grant MH 33990 and a grant from the W. T. Grant Foundation. Reprint requests to Dr. Bowring. WPiC, 3811 O'Hara Street, Pittsburgh, PA 15213. 0890-8567/92/3104-0611$03.00/0©1992 by the American Academy of Child and Adolescent Psychiatry.

Financiación

Financiadores	Número del financiador
Eunice Kennedy Shriver National Institute of Child Health and Human Development	R01HD029758

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.270.50.29640

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title = "Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family",

abstract = "Activation of phosphatidylcholine-specific phospholipase D (PLD) has been implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. We report here the identification of the first human PLD cDNA, which defines a new and highly conserved gene family. Characterization of recombinant human PLD1 reveals that it is membrane-associated, selective for phosphatidylcholine, stimulated by phosphatidylinositol 4,5-bisphosphate, activated by the monomeric G-protein ADP-ribosylation factor-1, and inhibited by oleate. PLD1 likely encodes the gene product responsible for the most widely studied endogenous PLD activity.",

author = "Hammond, \{Scott M.\} and Altshuller, \{Yelena M.\} and Sung, \{Tsung Chang\} and Rudge, \{Simon A.\} and Kristine Rose and Engebrecht, \{Jo Anne\} and Morris, \{Andrew J.\} and Frohman, \{Michael A.\}",

note = "Funding Information: Accepted Januaty 9. 1992. From the Department ofPsychiatry, University ofPittsburgh School of Medicine, and the Western Psychiatric Institute and Clinic, Pittsburgh, PA. Preparation of this article was supported in part by NIMH grant MH 33990 and a grant from the W. T. Grant Foundation. Reprint requests to Dr. Bowring. WPiC, 3811 O'Hara Street, Pittsburgh, PA 15213. 0890-8567/92/3104-0611\$03.00/0{\textcopyright}1992 by the American Academy of Child and Adolescent Psychiatry.",

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T1 - Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family

AU - Hammond, Scott M.

AU - Altshuller, Yelena M.

AU - Sung, Tsung Chang

AU - Rudge, Simon A.

AU - Rose, Kristine

AU - Engebrecht, Jo Anne

AU - Morris, Andrew J.

AU - Frohman, Michael A.

N1 - Funding Information: Accepted Januaty 9. 1992. From the Department ofPsychiatry, University ofPittsburgh School of Medicine, and the Western Psychiatric Institute and Clinic, Pittsburgh, PA. Preparation of this article was supported in part by NIMH grant MH 33990 and a grant from the W. T. Grant Foundation. Reprint requests to Dr. Bowring. WPiC, 3811 O'Hara Street, Pittsburgh, PA 15213. 0890-8567/92/3104-0611$03.00/0©1992 by the American Academy of Child and Adolescent Psychiatry.

PY - 1995/12/15

Y1 - 1995/12/15

N2 - Activation of phosphatidylcholine-specific phospholipase D (PLD) has been implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. We report here the identification of the first human PLD cDNA, which defines a new and highly conserved gene family. Characterization of recombinant human PLD1 reveals that it is membrane-associated, selective for phosphatidylcholine, stimulated by phosphatidylinositol 4,5-bisphosphate, activated by the monomeric G-protein ADP-ribosylation factor-1, and inhibited by oleate. PLD1 likely encodes the gene product responsible for the most widely studied endogenous PLD activity.

AB - Activation of phosphatidylcholine-specific phospholipase D (PLD) has been implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. We report here the identification of the first human PLD cDNA, which defines a new and highly conserved gene family. Characterization of recombinant human PLD1 reveals that it is membrane-associated, selective for phosphatidylcholine, stimulated by phosphatidylinositol 4,5-bisphosphate, activated by the monomeric G-protein ADP-ribosylation factor-1, and inhibited by oleate. PLD1 likely encodes the gene product responsible for the most widely studied endogenous PLD activity.

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Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family

Resumen

Nota bibliográfica

Financiación

ASJC Scopus subject areas

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