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PI4KB  -  phosphatidylinositol 4-kinase, catalytic,...

Homo sapiens

Synonyms: NPIK, PI4K-BETA, PI4K-beta, PI4K92, PI4KBETA, ...
 
 
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Disease relevance of PIK4CB

 

High impact information on PIK4CB

 

Biological context of PIK4CB

 

Anatomical context of PIK4CB

 

Associations of PIK4CB with chemical compounds

  • Recently we isolated a distinct human PtdIns 4-kinase gene, named PI4Kbeta, that encodes an enzyme that is wortmannin sensitive (Meyers, R., and Cantley, L. C. (1997) J. Biol. Chem. 272, 4384-4390) [10].
  • Recombinant NPIK protein catalyzed a conversion from phosphatidylinositol to phosphatidylinositol 4-phosphate [7].
  • The catalytic activity of NPIK was augmented by Triton X-100, and was reduced in the presence of adenosine [7].
  • Recombinant PI4Kbeta, but not its glutathione S-transferase-fused form, showed enhanced PI kinase activity when incubated with recombinant NCS-1, but only if the latter was myristoylated [8].
  • We show further that overexpression of NCS-1 in RBL-2H3 cells stimulates the catalytic activity of PI4Kbeta, increases IgE receptor (FcepsilonRI)-triggered hydrolysis of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)), and stimulates FcepsilonRI-triggered, but not Ca(2+) ionophore-triggered, exocytosis [12].
 

Physical interactions of PIK4CB

  • These results together indicate that NCS-1 is able to interact with PI4Kbeta also in mammalian cells and may play a role in the regulation of this enzyme in specific cellular compartments affecting vesicular trafficking [8].
 

Other interactions of PIK4CB

 

Analytical, diagnostic and therapeutic context of PIK4CB

  • Indirect immunofluorescence reveals that PI4K92 phosphorylated on Ser-294 localizes exclusively at the Golgi [4].
  • Microinjection of anti-pSer-496, but not of anti-pSer-294 or anti-pThr-504 antibody, into the cytoplasm or into the nucleus of HS68 cells leads to development of hotspots, probably representing aggregated PI4K92, and in later stages, cells become apoptotic and finally die [4].
  • The distribution and cellular localisation of the phosphatidylinositol 4-kinase isoforms, PI4K230 and PI4K92, that are believed to play important roles in the intracellular signalling mechanisms were studied in the rat brain (cortex, cerebellum, hippocampus and spinal cord) using immunocytochemistry with light and electron microscopy [16].

References

  1. Protein kinase D regulates vesicular transport by phosphorylating and activating phosphatidylinositol-4 kinase IIIbeta at the Golgi complex. Hausser, A., Storz, P., Märtens, S., Link, G., Toker, A., Pfizenmaier, K. Nat. Cell Biol. (2005) [Pubmed]
  2. Binding of Elongation Factor eEF1A2 to Phosphatidylinositol 4-Kinase beta Stimulates Lipid Kinase Activity and Phosphatidylinositol 4-Phosphate Generation. Jeganathan, S., Lee, J.M. J. Biol. Chem. (2007) [Pubmed]
  3. Neuronal calcium sensor-1 and phosphatidylinositol 4-kinase beta stimulate extracellular signal-regulated kinase 1/2 signaling by accelerating recycling through the endocytic recycling compartment. Kapp-Barnea, Y., Ninio-Many, L., Hirschberg, K., Fukuda, M., Jeromin, A., Sagi-Eisenberg, R. Mol. Biol. Cell (2006) [Pubmed]
  4. Subcellular localization and structural function of endogenous phosphorylated phosphatidylinositol 4-kinase (PI4K92). Szivak, I., Lamb, N., Heilmeyer, L.M. J. Biol. Chem. (2006) [Pubmed]
  5. A role for a wortmannin-sensitive phosphatidylinositol-4-kinase in the endocytosis of muscarinic cholinergic receptors. Sorensen, S.D., Linseman, D.A., McEwen, E.L., Heacock, A.M., Fisher, S.K. Mol. Pharmacol. (1998) [Pubmed]
  6. Human phosphatidylinositol 4-kinase isoform PI4K92. Expression of the recombinant enzyme and determination of multiple phosphorylation sites. Suer, S., Sickmann, A., Meyer, H.E., Herberg, F.W., Heilmeyer, L.M. Eur. J. Biochem. (2001) [Pubmed]
  7. Identification and characterization of a novel human phosphatidylinositol 4-kinase. Suzuki, K., Hirano, H., Okutomi, K., Suzuki, M., Kuga, Y., Fujiwara, T., Kanemoto, N., Isono, K., Horie, M. DNA Res. (1997) [Pubmed]
  8. Interaction of neuronal calcium sensor-1 (NCS-1) with phosphatidylinositol 4-kinase beta stimulates lipid kinase activity and affects membrane trafficking in COS-7 cells. Zhao, X., Várnai, P., Tuymetova, G., Balla, A., Tóth, Z.E., Oker-Blom, C., Roder, J., Jeromin, A., Balla, T. J. Biol. Chem. (2001) [Pubmed]
  9. Type II phosphatidylinositol 4-kinase beta is a cytosolic and peripheral membrane protein that is recruited to the plasma membrane and activated by Rac-GTP. Wei, Y.J., Sun, H.Q., Yamamoto, M., Wlodarski, P., Kunii, K., Martinez, M., Barylko, B., Albanesi, J.P., Yin, H.L. J. Biol. Chem. (2002) [Pubmed]
  10. Subcellular locations of phosphatidylinositol 4-kinase isoforms. Wong, K., Meyers ddR, n.u.l.l., Cantley, L.C. J. Biol. Chem. (1997) [Pubmed]
  11. Distinct Golgi populations of phosphatidylinositol 4-phosphate regulated by phosphatidylinositol 4-kinases. Weixel, K.M., Blumental-Perry, A., Watkins, S.C., Aridor, M., Weisz, O.A. J. Biol. Chem. (2005) [Pubmed]
  12. Neuronal calcium sensor-1 and phosphatidylinositol 4-kinase beta regulate IgE receptor-triggered exocytosis in cultured mast cells. Kapp-Barnea, Y., Melnikov, S., Shefler, I., Jeromin, A., Sagi-Eisenberg, R. J. Immunol. (2003) [Pubmed]
  13. Type I phosphatidylinositol 4-phosphate 5-kinase directly interacts with ADP-ribosylation factor 1 and is responsible for phosphatidylinositol 4,5-bisphosphate synthesis in the golgi compartment. Jones, D.H., Morris, J.B., Morgan, C.P., Kondo, H., Irvine, R.F., Cockcroft, S. J. Biol. Chem. (2000) [Pubmed]
  14. Type II phosphatidylinositol 4-kinase beta associates with TCR-CD3 zeta chain in Jurkat cells. Srivastava, R., Sinha, R.K., Subrahmanyam, G. Mol. Immunol. (2006) [Pubmed]
  15. Phospho-specific binding of 14-3-3 proteins to phosphatidylinositol 4-kinase III {beta} protects from dephosphorylation and stabilizes lipid kinase activity. Hausser, A., Link, G., Hoene, M., Russo, C., Selchow, O., Pfizenmaier, K. J. Cell. Sci. (2006) [Pubmed]
  16. Immunohistochemical localisation of two phosphatidylinositol 4-kinase isoforms, PI4K230 and PI4K92, in the central nervous system of rats. Balla, A., Vereb, G., Gülkan, H., Gehrmann, T., Gergely, P., Heilmeyer, L.M., Antal, M. Experimental brain research. Experimentelle Hirnforschung. Expérimentation cérébrale. (2000) [Pubmed]
 
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