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PLD2 protein itself interacts with HIF-1alpha (show HIF1A Proteins), prolyl hydroxylase (PHD (show PDC Proteins)) and VHL (show VHL Proteins) to promote degradation of HIF-1alpha (show HIF1A Proteins) via the proteasomal pathway independent of lipase (show LIPG Proteins) activity.
PLD2-mediated production of phosphatidic acid contributed to the control of EGFR (show EGFR Proteins) exposure to ligand through a multipronged transcriptional and posttranscriptional program during the out-of-control accumulation of EGFR (show EGFR Proteins) signaling in cancer cells.
These results suggest that PLD2 expression in colon cancer cells is up-regulated via HIF1-alpha (show HIF1A Proteins) in response to hypoxic stress and underscores the crucial role of HIF1-alpha (show HIF1A Proteins)-induced PLD2 in tumor growth.
A 3D model of the PLD2 by combining homology and ab initio 3 dimensional structural modeling methods, and docking conformation, is reported.
PLD2 expression regulates formation of Golgi tubules in Hela cells.
Results indicate distinctive roles of phospholipase D PLD1 and PLD2 isoforms in pathological conditions in retinal pigment epithelium (RPE).
Phospholipase D is involved in the formation of Golgi associated clathrin coated vesicles in human parotid duct cells
PLD2, but not PLD1, directly binds to the C terminus of TREK1 (show KCNK2 Proteins) and TREK2 (show KCNK10 Proteins).
Ectopic expression of PLD1 or PLD2 in human glioma U87 cells increased the expression of hypoxia-inducible factor-1alpha protein.
Knockdown of PLD2 induces autophagy in colorectal cancer cells.
Results suggest that PLD2 is the isoform that mediates aldosterone secretion and likely priming.
PLD1/2 signaling pathways are involved in mitogenic signaling in astrocytes.
Data show that although phospholipase D PLD1 deficiency impaired Fc epsilon receptor FcepsilonRI-mediated signaling and mast cell function, phospholipase D PLD2 deficiency actually enhanced these pathways.
PLD2 in neutrophils is essential for the pathogenesis of experimental sepsis
The impact of polyunsaturated fatty acid (PUFA) supplementation on phospholipase D (PLD) trafficking and activity in mast cells was investigated.
AQP3 (show AQP3 Proteins) has a pro-differentiative role in epidermal keratinocytes and PLD2 activity is necessary for this effect.
phosphatidic acid and phospholipase D1 and D2 have roles in leukocyte adhesion
PLD1 and PLD2 have roles in platelet alpha-granule secretion
Demonstrate a novel role for endothelial PLD2 in the survival and migration of ECs under hypoxia via the expression of hypoxia-inducible factor-1alpha and in pathological retinal angiogenesis and tumor angiogenesis in vivo.
Pharmacological PLD inhibition might provide a safe therapeutic strategy to prevent arterial thrombosis and ischemic stroke.
PLD2 is a unique GEF (show ARHGEF2 Proteins), with the PX being the major catalytic domain for its GEF (show ARHGEF2 Proteins) activity, whereas the pleckstrin (show PLEK Proteins) homology domain assists in the PX-mediated activity
The results indicate that PKC (show FYN Proteins) could be the final target and an integrator molecule of different signaling pathways triggered by angiotensin II (Ang II), which could explain the sustained activation of Na(+)-ATPase by Ang II (show AGT Proteins).
The protein encoded by this gene catalyzes the hydrolysis of phosphatidylcholine to phosphatidic acid and choline. The activity of the encoded enzyme is enhanced by phosphatidylinositol 4,5-bisphosphate and ADP-ribosylation factor-1. This protein localizes to the peripheral membrane and may be involved in cytoskeletal organization, cell cycle control, transcriptional regulation, and/or regulated secretion. Two transcript variants encoding different isoforms have been found for this gene.
, phospholipase D2-like
, choline phosphatase 2
, phosphatidylcholine-hydrolyzing phospholipase D2
, PLD 2
, phospholipase D gene 2