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Propose that MIGA proteins promote mitochondrial fusion by regulating mitochondrial phospholipid metabolism via MitoPLD (show PLD6 Antibodies).
The results suggest that Pld functions to promote trafficking of Golgi-derived fusion-competent vesicles during cellularization.
In Arabidopsis thaliana, PLDalpha1/PA might regulate cell development by modulating microtubule organization in an activity-dependent manner.
The phospholipase Dalpha1 protein is a key component and modulator of the G-protein complex in affecting a subset of signaling pathways.
PLDalpha1 and phosphatidic acid regulate microtubular organization and Ca(2 (show CA2 Antibodies)+) increases during abscisic acid (ABA)-induced stomatal closing and that crosstalk among signaling lipid, Ca(2 (show CA2 Antibodies)+), and microtubules is essential for ABA signaling.
Ablation of guard cell-expressed copper amine oxidase (show AOC3 Antibodies) gamma or phospholipase Dalpha1 gene retarded abscisic acid-induced H2O2 generation and stomatal closure.
ACBP1 interacts with PLDalpha1 at the plasma membrane. Their interaction was further confirmed by yeast two-hybrid analysis. As recombinant ACBP1 binds phosphatidic acid and phosphatidylcholine (show SGMS1 Antibodies), ACBP1 probably promotes PLDalpha1 action.
PLDalpha1-derived phosphatidic acid (PA) binds to MAP65-1, thus mediating microtubule stabilization and salt tolerance. It reveals a functional connection between membrane lipids and the cytoskeleton in environmental stress signaling.
PLDalpha1 and PLDdelta are involved in reactive oxygen species and nitric oxide production and cytosolic alkalization. PLDalpha1 and PLDdelta cooperate in ABA signaling in guard cells.
SPHK (show SPHK1 Antibodies)/phyto-S1P (show MBTPS1 Antibodies) and PLDalpha1A are co-dependent in amplification of response to ABA, mediating stomatal closure in Arabidopsis.
Piriformospora indica-stimulated growth response is mediated by a pathway consisting of the PLD-PDK1-OXI1 cascade.
PLDalpha1 mediates the abscisic acid effects on stomata through interaction with a protein phosphatase 2C & a heterotrimeric GTP-binding protein
Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes, including phytohormone action and response to stress, characterized by acidification of the cell.
, phospholipase D
, phospholipase d