Mammalian phospholipase D structure and regulation

Michael A. Frohman; Tsung Chang Sung; Andrew J. Morris

doi:10.1016/S1388-1981(99)00093-1

Mammalian phospholipase D structure and regulation

Michael A. Frohman
, Tsung Chang Sung
, Andrew J. Morris

Pharmacological Sciences

Stony Brook University

Research output: Contribution to journal › Review article › peer-review

287 Scopus citations

Abstract

The recent identification of cDNA clones for phospholipase D1 and 2 has opened the door to new studies on its structure and regulation. PLD activity is 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 multiple specialized steps in receptor dependent and constitutive processes of secretion, endocytosis, and membrane biogenesis. Copyright (C) 1999 Elsevier Science B.V.

Original language	English
Pages (from-to)	175-186
Number of pages	12
Journal	Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Volume	1439
Issue number	2
DOIs	https://doi.org/10.1016/S1388-1981(99)00093-1
State	Published - Jul 30 1999

Keywords

Catalytic domain
HKD motif
Phospholipase D structure

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10.1016/S1388-1981(99)00093-1

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abstract = "The recent identification of cDNA clones for phospholipase D1 and 2 has opened the door to new studies on its structure and regulation. PLD activity is 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 multiple specialized steps in receptor dependent and constitutive processes of secretion, endocytosis, and membrane biogenesis. Copyright (C) 1999 Elsevier Science B.V.",

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AU - Sung, Tsung Chang

AU - Morris, Andrew J.

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N2 - The recent identification of cDNA clones for phospholipase D1 and 2 has opened the door to new studies on its structure and regulation. PLD activity is 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 multiple specialized steps in receptor dependent and constitutive processes of secretion, endocytosis, and membrane biogenesis. Copyright (C) 1999 Elsevier Science B.V.

AB - The recent identification of cDNA clones for phospholipase D1 and 2 has opened the door to new studies on its structure and regulation. PLD activity is 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 multiple specialized steps in receptor dependent and constitutive processes of secretion, endocytosis, and membrane biogenesis. Copyright (C) 1999 Elsevier Science B.V.

KW - Catalytic domain

KW - HKD motif

KW - Phospholipase D structure

UR - https://www.scopus.com/pages/publications/0032810278

U2 - 10.1016/S1388-1981(99)00093-1

DO - 10.1016/S1388-1981(99)00093-1

M3 - Review article

C2 - 10425394

AN - SCOPUS:0032810278

SN - 1388-1981

VL - 1439

SP - 175

EP - 186

JO - Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

JF - Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

IS - 2

ER -

Mammalian phospholipase D structure and regulation

Abstract

Keywords

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