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Cited by 514

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Phospholipase D: molecular and cell biology of a novel gene family

Open access
Mordechai Liscovitch, Malgorzata Czarny, Giusy Fiucci, Xiaoqing Tang·2000·Biochemical Journal

Abstract

Interaction of extracellular-signal molecules with cell-surface receptors often activates a phospholipase D (PLD)-mediated hydrolysis of phosphatidylcholine and other phospholipids, generating phosphatidic acid. The activation of PLD is believed to play an important role in the regulation of cell function and cell fate. Multiple PLD activities were characterized in eukaryotic cells, and, more recently, several PLD genes have been cloned. A PLD gene superfamily, defined by a number of structural domains and sequence motifs, also includes phosphatidyltransferases and certain phosphodiesterases. Among the eukaryotic PLD genes are those from mammals, nematodes, fungi and plants. The present review focuses on the structure, localization, regulation and possible functions of cloned mammalian and yeast PLDs. In addition, an overview of plant PLD genes, and of several distinct PLD activities that have not yet been cloned, is provided. Emerging evidence from recent work employing new molecular tools indicates that different PLD isoforms are localized in distinct cellular organelles, where they are likely to serve diverse functions in signal transduction, membrane vesicle trafficking and cytoskeletal dynamics.

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OpenAlex · 10.1042/0264-6021:3450401

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Metadata

Authors
Liscovitch, M., Czarny, M., Fiucci, G., & Tang, X.
Venue
Biochemical Journal
Publisher
Portland Press
Published
2000-01-25
Volume
345
Issue
3
Pages
401-401
ISSN
0264-6021 (ISSN-L)
OpenAlex
W2066833882
Cited by
514
References
3
FWCI
28.85
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Phospholipase D: molecular and cell biology of a novel gene family. https://app.cochat.ai/papers/10.1042/0264-6021:3450401
The paper
Liscovitch, M., Czarny, M., Fiucci, G., & Tang, X. (2000). Phospholipase D: molecular and cell biology of a novel gene family. Biochemical Journal. https://doi.org/10.1042/0264-6021%3A3450401

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.