Topic
PLCD1
About: PLCD1 is a research topic. Over the lifetime, 29 publications have been published within this topic receiving 865 citations. The topic is also known as: NDNC3 & PLC-III.
Papers
TL;DR: The yeast SP014 gene, which is essential for meiosis, encodes a phospholipase D that has properties similar to mammalian phosphatidylinositol 4,5-bisphosphate-regulated phospholIPase D, and characterization of an unusual allele of SP014 defines regions of the protein important for enzyme catalysis and regulation.
Abstract: Phospholipid metabolism plays an important role in cellular regulation by generating second messengers for signal transduction. Many stimuli activate a phospholipase D, which catalyzes the hydrolysis of phosphatidylcholine, producing phosphatidic acid and choline. Here we report that the yeast SP014 gene, which is essential for meiosis [Honigberg, S. M., Conicella, C. & Esposito, R. E. (1992) Genetics 130, 703-716], encodes a phospholipase D. SP014 RNA and protein activity are induced during late meiotic prophase, and the enzyme has properties similar to mammalian phosphatidylinositol 4,5-bisphosphate-regulated phospholipase D. Characterization of an unusual allele of SP014 defines regions of the protein important for enzyme catalysis and regulation. These results implicate phospholipase D signaling in regulating cellular differentiation.
210 citations
TL;DR: The ratio of the activity of the activator to that of the phosphodiesterase varied greatly from tissue to tissue as well as during development, suggesting that the two proteins are under separate genetic control.
199 citations
TL;DR: While yeast contain multiple phospholipase D activities, only one, encoded by SPO14, appears to be a member of the phosphatidylcholine-specific phospholIPase D gene family.
40 citations
TL;DR: The findings suggest that PLCD1 acts as a tumour suppressor, by KIF3A-mediated suppression of ERK1/2/β-catenin/MMP7 signalling, at least in part, in breast cancer.
Abstract: Phospholipase C δ1 (PLCD1) encodes an enzyme involved in energy metabolism, calcium homeostasis and intracellular movement. It is located at 3p22 in a region that is frequently deleted in multiple cancers, and the PLCD1 enzyme is a potential tumour suppressor in breast cancer that inhibits matrix metalloprotease (MMP) 7, but the detailed mechanism remains elusive. In this study, we found that PLCD1 was downregulated in breast cancers, and the gain-or-loss functional assay revealed that PLCD1 inhibited cell migration and invasion in vitro via the ERK1/2/β-catenin/MMP7 signalling pathway. Furthermore, KIF3A was identified as a downstream mediator of PLCD1, and there was an inverse correlation between the expression of PLCD1 and KIF3A. Knockdown of KIF3A expression alone suppressed cell migration and invasion, and attenuated ERK1/2/β-catenin/MMP7 signalling that was reactivated by knocking down PLCD1 in vitro. Collectively, our findings suggest that PLCD1 acts as a tumour suppressor, by KIF3A-mediated suppression of ERK1/2/β-catenin/MMP7 signalling, at least in part, in breast cancer.
33 citations
TL;DR: This work has introduced multiple copies of the cloned phosphodiesterase gene into mutant amoebae and restored aggregation and the formation of anatomically correct fruiting bodies by transformation with the gene.
27 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2021 | 1 |
| 2019 | 1 |
| 2018 | 1 |
| 2017 | 1 |
| 2014 | 2 |
| 2012 | 2 |