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FAK sustained the active integrin conformation by maintaining talin association with Rab11 endosomes in a type I phosphatidylinositol phosphate kinase (PIPKIgamma)-dependent manner.
These data suggest that S6K1 (show RPS6KB1 Proteins)-mediated PIPKIgamma90 phosphorylation regulates cell migration and invasion by controlling PIPKIgamma90 degradation.
PIPKIgammai5, NEDD4-1 (show NEDD4 Proteins), and Mig6 (show ERRFI1 Proteins) form a novel molecular nexus that controls EGFR (show EGFR Proteins) activation and downstream signaling.
PIPKIgamma and INPP5E localize to the centrosome and coordinate the initiation of ciliogenesis.
results suggested that Akt (show AKT1 Proteins)-mediated PIP5Kgamma90 S555 phosphorylation is a novel regulatory point for talin binding to control PIP2 level at the FAs (show FAS Proteins), thereby modulating FA dynamics and cell motility.
Loss of PIPKIgamma or its focal adhesion-targeting variant, PIPKIgammai2, impaired PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins) activation upon stimulation with growth factors or extracellular matrix proteins in different tumor cells.
PIPKIgamma binds to the cryptic polo-box domain of PLK4 (show PLK4 Proteins) and reduces the kinase activity of PLK4 (show PLK4 Proteins).
This study uncovers a novel mechanism where a phosphoinositide-synthesizing enzyme, PIPKIgammai2, functions with the proto-oncogene (show RAB1A Proteins) Src (show SRC Proteins), to regulate oncogenic signaling
PIPKIgamma and phosphatidyl inositol phosphate pools at nascent E-cadherin (show CDH1 Proteins) contacts cue Exo70 (show EXOC7 Proteins) targeting and orient the tethering of exocyst-associated E-cadherin (show CDH1 Proteins)
PIPKIgamma positively regulates focal adhesion dynamics and cancer invasion, most probably through PIP (show PIP Proteins)-mediated vinculin (show VCL Proteins) activation.
Pip5k1a activity is regulated by dimerization and binding with the DIX domain of dishevelled (show DVL2 Proteins).
PIPKIgamma and INPP5E (show INPP5E Proteins) localize to the centrosome and coordinate the initiation of ciliogenesis.
PIPKIgamma, downstream of EGF (show EGF Proteins) and/or HGF receptor, participates in breast cancer progression
Shp1 binds and controls PIPKIgamma activity and, thereby, modulates phosphatidylinositol (4,5)-bisphosphate levels and adhesion.
The results of this study suggest that PIP5KIgamma, especially PIP5KIgamma_i2, is localized at the periactive zone, a functionally suitable compartment for the endocytosis of synaptic vesicles in photoreceptor ribbon synapses.
The lipid kinase PIP5K1C regulates pain signaling and sensitization in mice.
The findings suggest an essential role of PIP5KIgamma, particularly PIP5KIgamma_i2, in neuronal migration, possibly through recruitment of adhesion components to the plasma membrane.
Although PIP5KIgamma is essential for normal platelet function, individual isoforms of PIP5KIgamma fulfill unique roles for the integrin-dependent integrity of the membrane cytoskeleton and for the stabilization of platelet adhesion.
NMDA receptor activation controls AMPA AMPA AMPA (show GRIA3 Proteins) receptor endocytosis during hippocampal LTD by regulating PIP5Kgamma661 activity at postsynapses.
PIP5KIgamma-mediated generation of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) at sites of N-cadherin (show CDH2 Proteins) contacts regulates intercellular adhesion strength, an effect due in part to PI(4,5)P2-mediated regulation of gelsolin (show GSN Proteins).
PIP5K1C-90 polarization was required for polarized RhoA activation at uropods and provided an initial directional cue for neutrophil polarization on the endothelium.
This locus encodes a type I phosphatidylinositol 4-phosphate 5-kinase. The encoded protein catalyzes phosphorylation of phosphatidylinositol 4-phosphate, producing phosphatidylinositol 4,5-bisphosphate. This enzyme is found at synapses and has been found to play roles in endocytosis and cell migration. Mutations at this locus have been associated with lethal congenital contractural syndrome. Alternatively spliced transcript variants encoding different isoforms have been described.
Human homolog of mouse phosphatidylinositol-4-phosphate 5-kinase I-gamma
, diphosphoinositide kinase
, phosphatidylinositol 4-phosphate 5-kinase type I gamma
, phosphatidylinositol 4-phosphate 5-kinase type-1 gamma
, phosphatidylinositol-4-phosphate 5-kinase type-1 gamma
, ptdIns(4)P-5-kinase 1 gamma
, type I PIP kinase
, phosphatidylinositol-4-phosphate 5-kinase, type 1 gamma
, ptdIns(4)P-5-kinase gamma
, phosphatidylinositol-4-phosphate 5-kinase, type I, gamma
, phosphatidylinositol-4-phosphate 5-kinase type I gamma