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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 29640-29643 |
| Number of pages | 4 |
| Journal | Journal of Biological Chemistry |
| Volume | 270 |
| Issue number | 50 |
| DOIs | |
| State | Published - Dec 15 1995 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family. / Hammond, Scott M.; Altshuller, Yelena M.; Sung, Tsung Chang; Rudge, Simon A.; Rose, Kristine; Engebrecht, JoAnne; Morris, Andrew J.; Frohman, Michael A.
In: Journal of Biological Chemistry, Vol. 270, No. 50, 15.12.1995, p. 29640-29643.Research output: Contribution to journal › Article
}
TY - JOUR
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, JoAnne
AU - Morris, Andrew J.
AU - Frohman, Michael A.
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.
UR - http://www.scopus.com/inward/record.url?scp=0029564902&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0029564902&partnerID=8YFLogxK
U2 - 10.1074/jbc.270.50.29640
DO - 10.1074/jbc.270.50.29640
M3 - Article
C2 - 8530346
AN - SCOPUS:0029564902
VL - 270
SP - 29640
EP - 29643
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 50
ER -