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Gene Review:

pld-1 - Protein PLD-1

Caenorhabditis elegans

Min, D.S. et al., Liscovitch, M. et al., Harnett, M.M. et al., Lee, J.S. et al.

Min, Cho, Yoon, Lee, Hahn, Lee, Kim, Jo,

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Disease relevance of pld-1

Carbachol (CCh) induced inositol phosphate formation and a significantly higher Ca(2+) elevation and stimulated PLD activity through the mAChR; this was insensitive to pertussis toxin, but its activity was abolished by the phospholipase C (PLC) inhibitor U73122 [1].

High impact information on pld-1

Phospholipase C, protein kinase C, Ca(2+)/calmodulin-dependent protein kinase II, and tyrosine phosphorylation are involved in carbachol-induced phospholipase D activation in Chinese hamster ovary cells expressing muscarinic acetylcholine receptor of Caenorhabditis elegans [1].
Moreover, the Ca(2+)-calmodulin-dependent protein kinase II (CaM kinase II) inhibitor KN62, in addition to chelation of extracellular or intracellular Ca(2+) by EGTA and BAPTA/AM, abolished CCh-induced PLD activation and protein tyrosine phosphorylation [1].
Multiple PLD activities were characterized in eukaryotic cells, and, more recently, several PLD genes have been cloned [2].
To investigate the regulation of phospholipase D (PLD) signaling via a muscarinic receptor, we generated stable transfected Chinese hamster ovary (CHO) cells that overexpress the mAChR of C. elegans (CHO-GAR-3) [1].
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 [2].

Biological context of pld-1

Phytosphingosine and C2-phytoceramide induce cell death and inhibit carbachol-stimulated phospholipase D activation in Chinese hamster ovary cells expressing the Caenorhabditis elegans muscarinic acetylcholine receptor [3].

Associations of pld-1 with chemical compounds

In particular, ES-62 acts by modulating activation of the tyrosine kinases Fyn, Lck and ZAP-70 leading to selective disruption of TCR coupling to the phospholipase D, protein kinase C, phosphoinositide-3-kinase and RasMAPkinase signalling cascades [4].

References

Phospholipase C, protein kinase C, Ca(2+)/calmodulin-dependent protein kinase II, and tyrosine phosphorylation are involved in carbachol-induced phospholipase D activation in Chinese hamster ovary cells expressing muscarinic acetylcholine receptor of Caenorhabditis elegans. Min, D.S., Cho, N.J., Yoon, S.H., Lee, Y.H., Hahn, S.J., Lee, K.H., Kim, M.S., Jo, Y.H. J. Neurochem. (2000) [Pubmed]
Phospholipase D: molecular and cell biology of a novel gene family. Liscovitch, M., Czarny, M., Fiucci, G., Tang, X. Biochem. J. (2000) [Pubmed]
Phytosphingosine and C2-phytoceramide induce cell death and inhibit carbachol-stimulated phospholipase D activation in Chinese hamster ovary cells expressing the Caenorhabditis elegans muscarinic acetylcholine receptor. Lee, J.S., Min, D.S., Park, C., Park, C.S., Cho, N.J. FEBS Lett. (2001) [Pubmed]
Induction of signalling anergy via the T-cell receptor in cultured Jurkat T cells by pre-exposure to a filarial nematode secreted product. Harnett, M.M., Deehan, M.R., Williams, D.M., Harnett, W. Parasite Immunol. (1998) [Pubmed]

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PLDP1	Arabidopsis thaliana
PLDP2	Arabidopsis thaliana
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PLD1	Canis lupus familiaris
pld1b	Danio rerio
pld1a	Danio rerio
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PLD1	Homo sapiens
PLD1	Macaca mulatta
Pld1	Mus musculus
PLD1	Pan troglodytes
Pld1	Rattus norvegicus
pld1	Xenopus (Silurana) tropicalis

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