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Cloning of pip5k3 and report on its molecular characterization and expression pattern in adult fish as well as during development.
this study shows that PIKfyve coordinates the neutrophil immune response through the activation of the Rac (show AKT1 Proteins) GTPase (show RACGAP1 Proteins)
in PC-3 (show PCSK1 Proteins) cells inhibition of PIKfyve by apilimod or depletion by siRNA increased the secretion of the exosomal fraction.
Here we identify the lipid kinase PIKfyve as a regulator of an alternative pathway that distributes engulfed contents in support of intracellular macromolecular synthesis during macropinocytosis, entosis, and phagocytosis. We find that PIKfyve regulates vacuole size in part through its downstream effector, the cationic transporter TRPML1 (show MCOLN1 Proteins)
A cell-permeable tool for analysing APP (show APP Proteins) intracellular domain function and manipulation of PIKfyve activity.
A novel heterozygous frameshift mutation (c.3151dupA) and a copy number variations in PIKFYVE gene have been found in two unrelated Fleck corneal dystrophy patients.
The PIKfyve complex is required for APP (show APP Proteins) trafficking, suggesting a feedback loop in which APP (show APP Proteins), by binding to and stimulating phosphatidylinositol-3,5-bisphosphate vesicle formation may control its own trafficking.
APP (show APP Proteins) functionally cooperates with PIKfyve in vivo. This regulation is required for maintaining endosomal and neuronal function.
data identify a novel role of the ArPIKfyve (show VAC14 Proteins)-Sac3 (show MCM3AP Proteins) complex in the mechanisms controlling aggregate formation of Sph1 and suggest that Sac3 (show MCM3AP Proteins) protein deficiency or overproduction may facilitate aggregation of aggregation-prone proteins
Data suggest PIKFYVE, MTMR3 (myotubularin related protein 3 (show MTMR3 Proteins)) and their product phosphatidylinositol 5-phosphate are involved in activation of RAC1 (rho family small GTP binding protein (show ARF3 Proteins)); this process regulates migration/invasion of carcinoma/sarcoma.
Data indicate that pharmacological or genetic inactivation of PIKfyve rapidly induces expression of the transcription repressor ATF3 (show ATF3 Proteins), which is necessary and sufficient for suppression of type I IFN expression.
The authors provide evidence that inactivation of PIKfyve by the selective inhibitor STA (show SULT2A1 Proteins) suppresses excessive mitochondrial reactive oxygen species production and apoptosis through a SIRT3 (show SIRT3 Proteins)-dependent pathway in cardiomyoblasts.
Thus, PIKfyve plays a role in preventing excessive lung inflammation through regulating alveolar macrophage function.
adipose tissue Pikfyve plays a key role in the mechanisms regulating glucose homeostasis and the PIKfyve pathway is critical in mammary epithelial differentiation during pregnancy and lactogenesis downstream of prolactin receptor (show PRLR Proteins) signaling.
AP-3 (show AP3B1 Proteins) recruitment to TLR9 (show TLR9 Proteins) endosomes was impaired by PIKfyve inhibition.
PIKfyve mediates vesicle motility through the regulation of vesicle integrity in neurons.
Loss of PIKfyve in platelets causes a lysosomal disease leading to inflammation and thrombosis in mice.
Vps34 (show PIK3C3 Proteins) is a main phosphatidylinositol 3-phosphate source for constitutive PIKfyve functionality.
Daam2-PIP5K function, application of which stimulates remyelination after white matter injury
Phosphorylated derivatives of phosphatidylinositol (PtdIns) regulate cytoskeletal functions, membrane trafficking, and receptor signaling by recruiting protein complexes to cell- and endosomal-membranes. Humans have multiple PtdIns proteins that differ by the degree and position of phosphorylation of the inositol ring. This gene encodes an enzyme (PIKfyve\; also known as phosphatidylinositol-3-phosphate 5-kinase type III or PIPKIII) that phosphorylates the D-5 position in PtdIns and phosphatidylinositol-3-phosphate (PtdIns3P) to make PtdIns5P and PtdIns(3,5)biphosphate. The D-5 position also can be phosphorylated by type I PtdIns4P-5-kinases (PIP5Ks) that are encoded by distinct genes and preferentially phosphorylate D-4 phosphorylated PtdIns. In contrast, PIKfyve preferentially phosphorylates D-3 phosphorylated PtdIns. In addition to being a lipid kinase, PIKfyve also has protein kinase activity. PIKfyve regulates endomembrane homeostasis and plays a role in the biogenesis of endosome carrier vesicles from early endosomes. Mutations in this gene cause corneal fleck dystrophy (CFD)\; an autosomal dominant disorder characterized by numerous small white flecks present in all layers of the corneal stroma. Histologically, these flecks appear to be keratocytes distended with lipid and mucopolysaccharide filled intracytoplasmic vacuoles. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
, phosphatidylinositol-3-phosphate/phosphatidylinositol 5-kinase, type III
, 1-phosphatidylinositol 3-phosphate 5-kinase
, phosphatidylinositol 3-phosphate 5-kinase type III
, type III PIP kinase
, zinc finger, FYVE domain containing 29
, FYVE finger-containing phosphoinositide kinase
, phosphatidylinositol-3-phosphate 5-kinase type III
, phosphatidylinositol-4-phosphate 5-kinase, type III