Interaction of extracellular-signal molecules with cell-surface receptors o
ften activates a phospholipase D (PLD)-mediated hydrolysis of phosphatidylc
holine and other phospholipids, generating phosphatidic acid. The activatio
n of PLD is believed to play an important role in the regulation of cell fu
nction and cell fate. Multiple PLD activities were characterized in eukaryo
tic cells, and, more recently, several PLD genes have been cloned. A PLD ge
ne superfamily, defined by a number of structural domains and sequence moti
fs, 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, regulat
ion and possible functions of cloned mammalian and yeast PLDs, In addition,
an overview of plant PLD genes, and of several distinct PLD activities tha
t have not yet been cloned, is provided. Emerging evidence from recent work
employing new molecular tools indicates that different PLD isoforms are lo
calized in distinct cellular organelles, where they are likely to serve div
erse functions iq signal transduction, membrane vesicle trafficking and cyt
oskeletal dynamics.