Mammalian phospholipase D structure and regulation

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

Research output: Contribution to journalReview articlepeer-review

277 Citations (SciVal)

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 languageEnglish
Pages (from-to)175-186
Number of pages12
JournalBiochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Volume1439
Issue number2
DOIs
StatePublished - Jul 30 1999

Bibliographical note

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.

Keywords

  • Catalytic domain
  • HKD motif
  • Phospholipase D structure

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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