Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta isoform is an
enzyme that in humans is encoded by the PIK3CBgene.[5][6]
Phosphoinositide 3-kinases (PI3Ks)
phosphorylate the 3-prime OH position of the
inositol ring of inositol lipids. They have been implicated as participants in
signaling pathways regulating cell growth by virtue of their activation in response to various
mitogenic stimuli. PI3Ks are composed of a 110-kD catalytic subunit, such as PIK3CB, and an 85-kD adaptor subunit (Hu et al., 1993).[supplied by OMIM][6]
Katada T, Kurosu H, Okada T, et al. (1999). "Synergistic activation of a family of phosphoinositide 3-kinase via G-protein coupled and tyrosine kinase-related receptors". Chem. Phys. Lipids. 98 (1–2): 79–86.
doi:
10.1016/S0009-3084(99)00020-1.
PMID10358930.
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.
PMID12960231.
S2CID11362623.
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.
doi:
10.1002/eji.1830270946.
PMID9341793.
S2CID33397908.
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.
doi:
10.1002/eji.1830271110.
PMID9394803.
S2CID6303471.
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.
doi:
10.1006/bbrc.1997.7877.
PMID9446795.
Steták A, Csermely P, Ullrich A, Kéri G (2001). "Physical and functional interactions between protein tyrosine phosphatase alpha, PI 3-kinase, and PKCdelta". Biochem. Biophys. Res. Commun. 288 (3): 564–72.
doi:
10.1006/bbrc.2001.5811.
PMID11676480.
Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta isoform is an
enzyme that in humans is encoded by the PIK3CBgene.[5][6]
Phosphoinositide 3-kinases (PI3Ks)
phosphorylate the 3-prime OH position of the
inositol ring of inositol lipids. They have been implicated as participants in
signaling pathways regulating cell growth by virtue of their activation in response to various
mitogenic stimuli. PI3Ks are composed of a 110-kD catalytic subunit, such as PIK3CB, and an 85-kD adaptor subunit (Hu et al., 1993).[supplied by OMIM][6]
Katada T, Kurosu H, Okada T, et al. (1999). "Synergistic activation of a family of phosphoinositide 3-kinase via G-protein coupled and tyrosine kinase-related receptors". Chem. Phys. Lipids. 98 (1–2): 79–86.
doi:
10.1016/S0009-3084(99)00020-1.
PMID10358930.
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.
PMID12960231.
S2CID11362623.
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.
doi:
10.1002/eji.1830270946.
PMID9341793.
S2CID33397908.
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.
doi:
10.1002/eji.1830271110.
PMID9394803.
S2CID6303471.
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.
doi:
10.1006/bbrc.1997.7877.
PMID9446795.
Steták A, Csermely P, Ullrich A, Kéri G (2001). "Physical and functional interactions between protein tyrosine phosphatase alpha, PI 3-kinase, and PKCdelta". Biochem. Biophys. Res. Commun. 288 (3): 564–72.
doi:
10.1006/bbrc.2001.5811.
PMID11676480.