RalA interacts directly with the Arf-responsive, PIP2-dependent phospholipase D1

Jing Qing Luo; Xin Liu; Scott M. Hammond; William C. Colley; Larry A. Feig; Michael A. Frohman; Andrew J. Morris; David A. Foster

doi:10.1006/bbrc.1997.6793

RalA interacts directly with the Arf-responsive, PIP₂-dependent phospholipase D1

Jing Qing Luo, Xin Liu, Scott M. Hammond, William C. Colley, Larry A. Feig, Michael A. Frohman, Andrew J. Morris, David A. Foster

Internal Medicine

Research output: Contribution to journal › Article › peer-review

79 Scopus citations

Abstract

RalA GTPase associates with a phospholipase D (PLD) that is activated in v-Src- and v-Ras-transformed cells. Two mammalian PLDs were recently cloned: PLD1, which is activated by Arf family GTPases and dependent upon phosphatidylinositol-4,5-bisphosphate (PIP₂), and PLD2, which is also dependent upon PIPE, but not stimulated by Arf. Another PLD has been described that is stimulated by oleate. Evidence is provided that the RalA-assiciated PLD is PLD1. First, the PLD precipitated by RalA from murine fibroblasts was stimulated by Arf, dependent upon PIP₂, and inhibited by oleate. Second, immobilized RalA precipitated PLD1 from sf9 insect cells overexpressing PLD1. Third, a series of RalA mutants precipitated PLD activity from both PLD1-expressing insect cells and murine fibroblasts with the same efficiency. And finally, immobilized RalA precipitated PLD1 from a purified PLD1 preparation. These data argue that RalA associates directly with the Arf-responsive, PIP₂-dependent PLD1.

Original language	English
Pages (from-to)	854-859
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	235
Issue number	3
DOIs	https://doi.org/10.1006/bbrc.1997.6793
State	Published - Jun 27 1997

Bibliographical note

Funding Information:
We are thankful to Paul Sternweis and Alex Brown for providing partially puri®ed native Arf protein. This investigation was supported by National Institutes of Health Grant CA46677, Council for Tobacco Research Grant 3075, American Cancer Society Grant BE-243 (to D.A.F.); a Research Centers in Minority Institutions award from the Division of Research Resources, National Institutes of Health (RR 03037) to Hunter College; National Institutes of Health Grant GM47707 and an American Cancer Society faculty research award (to L.A.F.); National Institutes of Health Grants GM50388 (to A.J.M.) and HD29758 (to M.A.F.). S.M.H. is a Pharmaceutical Manufacturers Foundation Predoctoral Fellow. X.L. was a Howard Hughes Medical Institute Undergraduate Scholar.

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1006/bbrc.1997.6793

Cite this

@article{34e18a081f50436abe15f4df9ec3e1ac,

title = "RalA interacts directly with the Arf-responsive, PIP2-dependent phospholipase D1",

abstract = "RalA GTPase associates with a phospholipase D (PLD) that is activated in v-Src- and v-Ras-transformed cells. Two mammalian PLDs were recently cloned: PLD1, which is activated by Arf family GTPases and dependent upon phosphatidylinositol-4,5-bisphosphate (PIP2), and PLD2, which is also dependent upon PIPE, but not stimulated by Arf. Another PLD has been described that is stimulated by oleate. Evidence is provided that the RalA-assiciated PLD is PLD1. First, the PLD precipitated by RalA from murine fibroblasts was stimulated by Arf, dependent upon PIP2, and inhibited by oleate. Second, immobilized RalA precipitated PLD1 from sf9 insect cells overexpressing PLD1. Third, a series of RalA mutants precipitated PLD activity from both PLD1-expressing insect cells and murine fibroblasts with the same efficiency. And finally, immobilized RalA precipitated PLD1 from a purified PLD1 preparation. These data argue that RalA associates directly with the Arf-responsive, PIP2-dependent PLD1.",

author = "Luo, {Jing Qing} and Xin Liu and Hammond, {Scott M.} and Colley, {William C.} and Feig, {Larry A.} and Frohman, {Michael A.} and Morris, {Andrew J.} and Foster, {David A.}",

note = "Funding Information: We are thankful to Paul Sternweis and Alex Brown for providing partially puri{\textregistered}ed native Arf protein. This investigation was supported by National Institutes of Health Grant CA46677, Council for Tobacco Research Grant 3075, American Cancer Society Grant BE-243 (to D.A.F.); a Research Centers in Minority Institutions award from the Division of Research Resources, National Institutes of Health (RR 03037) to Hunter College; National Institutes of Health Grant GM47707 and an American Cancer Society faculty research award (to L.A.F.); National Institutes of Health Grants GM50388 (to A.J.M.) and HD29758 (to M.A.F.). S.M.H. is a Pharmaceutical Manufacturers Foundation Predoctoral Fellow. X.L. was a Howard Hughes Medical Institute Undergraduate Scholar.",

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T1 - RalA interacts directly with the Arf-responsive, PIP2-dependent phospholipase D1

AU - Luo, Jing Qing

AU - Liu, Xin

AU - Hammond, Scott M.

AU - Colley, William C.

AU - Feig, Larry A.

AU - Frohman, Michael A.

AU - Morris, Andrew J.

AU - Foster, David A.

N1 - Funding Information: We are thankful to Paul Sternweis and Alex Brown for providing partially puri®ed native Arf protein. This investigation was supported by National Institutes of Health Grant CA46677, Council for Tobacco Research Grant 3075, American Cancer Society Grant BE-243 (to D.A.F.); a Research Centers in Minority Institutions award from the Division of Research Resources, National Institutes of Health (RR 03037) to Hunter College; National Institutes of Health Grant GM47707 and an American Cancer Society faculty research award (to L.A.F.); National Institutes of Health Grants GM50388 (to A.J.M.) and HD29758 (to M.A.F.). S.M.H. is a Pharmaceutical Manufacturers Foundation Predoctoral Fellow. X.L. was a Howard Hughes Medical Institute Undergraduate Scholar.

PY - 1997/6/27

Y1 - 1997/6/27

N2 - RalA GTPase associates with a phospholipase D (PLD) that is activated in v-Src- and v-Ras-transformed cells. Two mammalian PLDs were recently cloned: PLD1, which is activated by Arf family GTPases and dependent upon phosphatidylinositol-4,5-bisphosphate (PIP2), and PLD2, which is also dependent upon PIPE, but not stimulated by Arf. Another PLD has been described that is stimulated by oleate. Evidence is provided that the RalA-assiciated PLD is PLD1. First, the PLD precipitated by RalA from murine fibroblasts was stimulated by Arf, dependent upon PIP2, and inhibited by oleate. Second, immobilized RalA precipitated PLD1 from sf9 insect cells overexpressing PLD1. Third, a series of RalA mutants precipitated PLD activity from both PLD1-expressing insect cells and murine fibroblasts with the same efficiency. And finally, immobilized RalA precipitated PLD1 from a purified PLD1 preparation. These data argue that RalA associates directly with the Arf-responsive, PIP2-dependent PLD1.

AB - RalA GTPase associates with a phospholipase D (PLD) that is activated in v-Src- and v-Ras-transformed cells. Two mammalian PLDs were recently cloned: PLD1, which is activated by Arf family GTPases and dependent upon phosphatidylinositol-4,5-bisphosphate (PIP2), and PLD2, which is also dependent upon PIPE, but not stimulated by Arf. Another PLD has been described that is stimulated by oleate. Evidence is provided that the RalA-assiciated PLD is PLD1. First, the PLD precipitated by RalA from murine fibroblasts was stimulated by Arf, dependent upon PIP2, and inhibited by oleate. Second, immobilized RalA precipitated PLD1 from sf9 insect cells overexpressing PLD1. Third, a series of RalA mutants precipitated PLD activity from both PLD1-expressing insect cells and murine fibroblasts with the same efficiency. And finally, immobilized RalA precipitated PLD1 from a purified PLD1 preparation. These data argue that RalA associates directly with the Arf-responsive, PIP2-dependent PLD1.

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