PIK3C2B

From Wikipedia, the free encyclopedia

Phosphoinositide-3-kinase, class 2, beta polypeptide

Identifiers

PIK3C2B; C2-PI3K; DKFZp686G16234

External IDs

OMIM: 602838 MGI: 2685045 HomoloGene: 20582

Gene ontology
Molecular Function:	• inositol or phosphatidylinositol kinase activity • protein binding • kinase activity • 1-phosphatidylinositol-3-kinase activity • transferase activity • phosphatidylinositol-4-phosphate 3-kinase activity • phosphoinositide binding
Cellular Component:	• nucleus • microsome • cytosol • plasma membrane • phosphoinositide 3-kinase complex
Biological Process:	• cell communication • biological_process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_002646 (mRNA)
NP_002637 (protein)

XM_001001586 (mRNA)
XP_001001586 (protein)

Location

Chr 1: 202.66 - 202.73 Mb

Chr 1: 134.87 - 134.93 Mb

Pubmed search

[1]

[2]

Phosphoinositide-3-kinase, class 2, beta polypeptide, also known as PIK3C2B, is a human gene.^[1]

The protein encoded by this gene belongs to the phosphoinositide 3-kinase (PI3K) family. PI3-kinases play roles in signaling pathways involved in cell proliferation, oncogenic transformation, cell survival, cell migration, and intracellular protein trafficking. This protein contains a lipid kinase catalytic domain as well as a C-terminal C2 domain, a characteristic of class II PI3-kinases. C2 domains act as calcium-dependent phospholipid binding motifs that mediate translocation of proteins to membranes, and may also mediate protein-protein interactions. The PI3-kinase activity of this protein is sensitive to low nanomolar levels of the inhibitor wortmanin. The C2 domain of this protein was shown to bind phospholipids but not Ca2+, which suggests that this enzyme may function in a calcium-independent manner.^[1]

[edit] References

^ ^a ^b Entrez Gene: PIK3C2B phosphoinositide-3-kinase, class 2, beta polypeptide.

[edit] Further reading

Lee C, Liu QH, Tomkowicz B, et al. (2004). "Macrophage activation through CCR5- and CXCR4-mediated gp120-elicited signaling pathways.". J. Leukoc. Biol. 74 (5): 676–82. doi:10.1189/jlb.0503206. PMID 12960231.
Kozutsumi H, Toyoshima H, Hagiwara K, et al. (1994). "Human ltk receptor tyrosine kinase binds to PLC-gamma 1, PI3-K, GAP and Raf-1 in vivo.". Oncogene 9 (10): 2991–8. PMID 8084603.
Milani D, Mazzoni M, Borgatti P, et al. (1996). "Extracellular human immunodeficiency virus type-1 Tat protein activates phosphatidylinositol 3-kinase in PC12 neuronal cells.". J. Biol. Chem. 271 (38): 22961–4. PMID 8798481.
Brown RA, Ho LK, Weber-Hall SJ, et al. (1997). "Identification and cDNA cloning of a novel mammalian C2 domain-containing phosphoinositide 3-kinase, HsC2-PI3K.". Biochem. Biophys. Res. Commun. 233 (2): 537–44. doi:10.1006/bbrc.1997.6495. PMID 9144573.
Ueno H, Honda H, Nakamoto T, et al. (1997). "The phosphatidylinositol 3' kinase pathway is required for the survival signal of leukocyte tyrosine kinase.". Oncogene 14 (25): 3067–72. doi:10.1038/sj.onc.1201153. PMID 9223670.
Mazerolles F, Barbat C, Fischer A (1997). "Down-regulation of LFA-1-mediated T cell adhesion induced by the HIV envelope glycoprotein gp160 requires phosphatidylinositol-3-kinase activity.". Eur. J. Immunol. 27 (9): 2457–65. PMID 9341793.
Borgatti P, Zauli G, Colamussi ML, et al. (1998). "Extracellular HIV-1 Tat protein activates phosphatidylinositol 3- and Akt/PKB kinases in CD4+ T lymphoblastoid Jurkat cells.". Eur. J. Immunol. 27 (11): 2805–11. PMID 9394803.
Borgatti P, Zauli G, Cantley LC, Capitani S (1998). "Extracellular HIV-1 Tat protein induces a rapid and selective activation of protein kinase C (PKC)-alpha, and -epsilon and -zeta isoforms in PC12 cells.". Biochem. Biophys. Res. Commun. 242 (2): 332–7. PMID 9446795.
Milani D, Mazzoni M, Zauli G, et al. (1998). "HIV-1 Tat induces tyrosine phosphorylation of p125FAK and its association with phosphoinositide 3-kinase in PC12 cells.". AIDS 12 (11): 1275–84. PMID 9708406.
Jauliac S, Mazerolles F, Jabado N, et al. (1998). "Ligands of CD4 inhibit the association of phospholipase Cgamma1 with phosphoinositide 3 kinase in T cells: regulation of this association by the phosphoinositide 3 kinase activity.". Eur. J. Immunol. 28 (10): 3183–91. PMID 9808187.
Arcaro A, Volinia S, Zvelebil MJ, et al. (1999). "Human phosphoinositide 3-kinase C2beta, the role of calcium and the C2 domain in enzyme activity.". J. Biol. Chem. 273 (49): 33082–90. PMID 9830063.
Arcaro A, Zvelebil MJ, Wallasch C, et al. (2000). "Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors.". Mol. Cell. Biol. 20 (11): 3817–30. PMID 10805725.
Park IW, Wang JF, Groopman JE (2001). "HIV-1 Tat promotes monocyte chemoattractant protein-1 secretion followed by transmigration of monocytes.". Blood 97 (2): 352–8. PMID 11154208.
Zauli G, Milani D, Mirandola P, et al. (2001). "HIV-1 Tat protein down-regulates CREB transcription factor expression in PC12 neuronal cells through a phosphatidylinositol 3-kinase/AKT/cyclic nucleoside phosphodiesterase pathway.". FASEB J. 15 (2): 483–91. doi:10.1096/fj.00-0354com. PMID 11156964.
Wheeler M, Domin J (2001). "Recruitment of the class II phosphoinositide 3-kinase C2beta to the epidermal growth factor receptor: role of Grb2.". Mol. Cell. Biol. 21 (19): 6660–7. PMID 11533253.
Deregibus MC, Cantaluppi V, Doublier S, et al. (2002). "HIV-1-Tat protein activates phosphatidylinositol 3-kinase/ AKT-dependent survival pathways in Kaposi's sarcoma cells.". J. Biol. Chem. 277 (28): 25195–202. doi:10.1074/jbc.M200921200. PMID 11994280.
Cook JA, August A, Henderson AJ (2002). "Recruitment of phosphatidylinositol 3-kinase to CD28 inhibits HIV transcription by a Tat-dependent mechanism.". J. Immunol. 169 (1): 254–60. PMID 12077252.
Arcaro A, Khanzada UK, Vanhaesebroeck B, et al. (2002). "Two distinct phosphoinositide 3-kinases mediate polypeptide growth factor-stimulated PKB activation.". EMBO J. 21 (19): 5097–108. PMID 12356726.
Visnjić D, Crljen V, Curić J, et al. (2002). "The activation of nuclear phosphoinositide 3-kinase C2beta in all-trans-retinoic acid-differentiated HL-60 cells.". FEBS Lett. 529 (2-3): 268–74. PMID 12372612.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.