Phospholipase D structure and regulation

Michael A. Frohman; Andrew J. Morris

doi:10.1016/S0009-3084(99)00025-0

Phospholipase D structure and regulation

Michael A. Frohman, Andrew J. Morris

Internal Medicine

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

103 Scopus citations

Abstract

The recent identification of cDNA clones for phospholipase D has opened the door to new types of investigations into its structure and regulation. PLD activity has been found to be encoded by at least two different genes that contain catalytic domains that relate their mechanism of action to phosphodiesterases. In vivo roles for PLD suggest that it may be important for multiples steps in regulated secretion and membrane biogenesis. Copyright (C) 1999 Elsevier Science Ireland Ltd.

Original language	English
Pages (from-to)	127-140
Number of pages	14
Journal	Chemistry and Physics of Lipids
Volume	98
Issue number	1-2
DOIs	https://doi.org/10.1016/S0009-3084(99)00025-0
State	Published - Apr 1999

Bibliographical note

Funding Information:
The authors thank laboratory members for critical reading of the manuscript. This work was supported by grants from the NIH to AIM (GM50388) and MAF (GM54813).

Keywords

ARF
PLD1
PLD2
Phospholipase D
Protein kinase C
Rho

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Organic Chemistry
Cell Biology

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10.1016/S0009-3084(99)00025-0

Cite this

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title = "Phospholipase D structure and regulation",

abstract = "The recent identification of cDNA clones for phospholipase D has opened the door to new types of investigations into its structure and regulation. PLD activity has been found to be encoded by at least two different genes that contain catalytic domains that relate their mechanism of action to phosphodiesterases. In vivo roles for PLD suggest that it may be important for multiples steps in regulated secretion and membrane biogenesis. Copyright (C) 1999 Elsevier Science Ireland Ltd.",

keywords = "ARF, PLD1, PLD2, Phospholipase D, Protein kinase C, Rho",

author = "Frohman, {Michael A.} and Morris, {Andrew J.}",

note = "Funding Information: The authors thank laboratory members for critical reading of the manuscript. This work was supported by grants from the NIH to AIM (GM50388) and MAF (GM54813).",

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AU - Morris, Andrew J.

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AB - The recent identification of cDNA clones for phospholipase D has opened the door to new types of investigations into its structure and regulation. PLD activity has been found to be encoded by at least two different genes that contain catalytic domains that relate their mechanism of action to phosphodiesterases. In vivo roles for PLD suggest that it may be important for multiples steps in regulated secretion and membrane biogenesis. Copyright (C) 1999 Elsevier Science Ireland Ltd.

KW - ARF

KW - PLD1

KW - PLD2

KW - Phospholipase D

KW - Protein kinase C

KW - Rho

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SN - 0009-3084

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SP - 127

EP - 140

JO - Chemistry and Physics of Lipids

JF - Chemistry and Physics of Lipids

IS - 1-2

ER -

Phospholipase D structure and regulation

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

Access to Document

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