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

Internal Medicine

Producción científica: Review article › revisión exhaustiva

287 Citas (Scopus)

Resumen

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.

Idioma original	English
Páginas (desde-hasta)	175-186
Número de páginas	12
Publicación	Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Volumen	1439
N.º	2
DOI	https://doi.org/10.1016/S1388-1981(99)00093-1
Estado	Published - jul 30 1999

Nota bibliográfica

Funding Information:
The authors thank lab members for critical reading of the manuscript. Work in the authors’ laboratories is supported by grants from the National Institutes of Health (GM50388 to A.J.M. and GM54813 to M.A.F.), the American Cancer Society, the American Heart Association, the National Parkinson’s Foundation, and the Parkinson’s Disease Foundation.

Financiación

The authors thank lab members for critical reading of the manuscript. Work in the authors’ laboratories is supported by grants from the National Institutes of Health (GM50388 to A.J.M. and GM54813 to M.A.F.), the American Cancer Society, the American Heart Association, the National Parkinson’s Foundation, and the Parkinson’s Disease Foundation.

Financiadores	Número del financiador
National Parkinson’s Foundation
National Institutes of Health (NIH)	GM54813
American Cancer Society
National Institute of General Medical Sciences	R01GM050388
American Heart Association
Parkinson’s Disease Foundation of India

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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title = "Mammalian phospholipase D structure and regulation",

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.",

keywords = "Catalytic domain, HKD motif, Phospholipase D structure",

author = "Frohman, \{Michael A.\} and Sung, \{Tsung Chang\} and Morris, \{Andrew J.\}",

note = "Funding Information: The authors thank lab members for critical reading of the manuscript. Work in the authors{\textquoteright} laboratories is supported by grants from the National Institutes of Health (GM50388 to A.J.M. and GM54813 to M.A.F.), the American Cancer Society, the American Heart Association, the National Parkinson{\textquoteright}s Foundation, and the Parkinson{\textquoteright}s Disease Foundation.",

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AU - Frohman, Michael A.

AU - Sung, Tsung Chang

AU - Morris, Andrew J.

N1 - Funding Information: The authors thank lab members for critical reading of the manuscript. Work in the authors’ laboratories is supported by grants from the National Institutes of Health (GM50388 to A.J.M. and GM54813 to M.A.F.), the American Cancer Society, the American Heart Association, the National Parkinson’s Foundation, and the Parkinson’s Disease Foundation.

PY - 1999/7/30

Y1 - 1999/7/30

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

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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

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Mammalian phospholipase D structure and regulation

Resumen

Nota bibliográfica

Financiación

ASJC Scopus subject areas

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