The Experts below are selected from a list of 133404 Experts worldwide ranked by ideXlab platform

Samantha Cooray - One of the best experts on this subject based on the ideXlab platform.

  • the pivotal role of phosphatidylinositol 3 kinase akt signal transduction in virus survival
    Journal of General Virology, 2004
    Co-Authors: Samantha Cooray
    Abstract:

    Over the course of evolution, viruses have developed the ability to modulate a variety of host cell signalling pathways. Inhibition of Apoptosis, in particular, has become recognized as an important contributory factor in virus survival. Apoptotic Inhibition contributes to the establishment of latent and chronic infections and has been implicated in viral oncogenesis. The phosphatidylinositol 3-kinase (PI3K)–Akt pathway is utilized by many cell types for Inhibition of Apoptosis and cellular survival. Virus modulation of this pathway provides an alternative to the expression of viral oncogenes or the direct Inhibition of pro-apoptotic proteins. It has become evident that many viruses require up-regulation of this pathway to sustain long-term infections and it is modulated, in some cases, by specific viral products to create an environment favourable for cellular transformation. In other cases, PI3K–Akt signalling simply helps to create an environment favourable for virus replication and virion assembly. This review details the modulation and function of PI3K–Akt signalling for virus survival.

Laurence A Lasky - One of the best experts on this subject based on the ideXlab platform.

  • interaction of the tumor suppressor pten mmac with a pdz domain of magi3 a novel membrane associated guanylate kinase
    Journal of Biological Chemistry, 2000
    Co-Authors: Yan Wu, Susan D. Spencer, Richard P. Laura, Qimin Gu, Donald Dowbenko, Laurence A Lasky
    Abstract:

    Abstract PTEN/MMAC is a phosphatase that is mutated in multiple human tumors. PTEN/MMAC dephosphorylates 3-phosphorylated phosphatidylinositol phosphates that activate AKT/protein kinase B (PKB) kinase activity. AKT/PKB is implicated in the Inhibition of Apoptosis, and cell lines and tumors with mutated PTEN/MMAC show increased AKT/PKB kinase activity and resistance to Apoptosis. PTEN/MMAC contains a PDZ domain-binding site, and we show here that the phosphatase binds to a PDZ domain ofmembrane-associated guanylate kinase with inverted orientation (MAGI) 3, a novel inverted membrane-associated guanylate kinase that localizes to epithelial cell tight junctions. Importantly, MAGI3 and PTEN/MMAC cooperate to modulate the kinase activity of AKT/PKB. These data suggest that MAGI3 allows for the juxtaposition of PTEN/MMAC to phospholipid signaling pathways involved with cell survival.

  • Interaction of the Tumor Suppressor PTEN/MMAC with a PDZ Domain of MAGI3, a Novel Membrane-associated Guanylate Kinase
    Journal of Biological Chemistry, 2000
    Co-Authors: Yan Wu, Susan D. Spencer, Richard P. Laura, Qimin Gu, Donald Dowbenko, Laurence A Lasky
    Abstract:

    Abstract PTEN/MMAC is a phosphatase that is mutated in multiple human tumors. PTEN/MMAC dephosphorylates 3-phosphorylated phosphatidylinositol phosphates that activate AKT/protein kinase B (PKB) kinase activity. AKT/PKB is implicated in the Inhibition of Apoptosis, and cell lines and tumors with mutated PTEN/MMAC show increased AKT/PKB kinase activity and resistance to Apoptosis. PTEN/MMAC contains a PDZ domain-binding site, and we show here that the phosphatase binds to a PDZ domain ofmembrane-associated guanylate kinase with inverted orientation (MAGI) 3, a novel inverted membrane-associated guanylate kinase that localizes to epithelial cell tight junctions. Importantly, MAGI3 and PTEN/MMAC cooperate to modulate the kinase activity of AKT/PKB. These data suggest that MAGI3 allows for the juxtaposition of PTEN/MMAC to phospholipid signaling pathways involved with cell survival.

Yan Wu - One of the best experts on this subject based on the ideXlab platform.

  • interaction of the tumor suppressor pten mmac with a pdz domain of magi3 a novel membrane associated guanylate kinase
    Journal of Biological Chemistry, 2000
    Co-Authors: Yan Wu, Susan D. Spencer, Richard P. Laura, Qimin Gu, Donald Dowbenko, Laurence A Lasky
    Abstract:

    Abstract PTEN/MMAC is a phosphatase that is mutated in multiple human tumors. PTEN/MMAC dephosphorylates 3-phosphorylated phosphatidylinositol phosphates that activate AKT/protein kinase B (PKB) kinase activity. AKT/PKB is implicated in the Inhibition of Apoptosis, and cell lines and tumors with mutated PTEN/MMAC show increased AKT/PKB kinase activity and resistance to Apoptosis. PTEN/MMAC contains a PDZ domain-binding site, and we show here that the phosphatase binds to a PDZ domain ofmembrane-associated guanylate kinase with inverted orientation (MAGI) 3, a novel inverted membrane-associated guanylate kinase that localizes to epithelial cell tight junctions. Importantly, MAGI3 and PTEN/MMAC cooperate to modulate the kinase activity of AKT/PKB. These data suggest that MAGI3 allows for the juxtaposition of PTEN/MMAC to phospholipid signaling pathways involved with cell survival.

  • Interaction of the Tumor Suppressor PTEN/MMAC with a PDZ Domain of MAGI3, a Novel Membrane-associated Guanylate Kinase
    Journal of Biological Chemistry, 2000
    Co-Authors: Yan Wu, Susan D. Spencer, Richard P. Laura, Qimin Gu, Donald Dowbenko, Laurence A Lasky
    Abstract:

    Abstract PTEN/MMAC is a phosphatase that is mutated in multiple human tumors. PTEN/MMAC dephosphorylates 3-phosphorylated phosphatidylinositol phosphates that activate AKT/protein kinase B (PKB) kinase activity. AKT/PKB is implicated in the Inhibition of Apoptosis, and cell lines and tumors with mutated PTEN/MMAC show increased AKT/PKB kinase activity and resistance to Apoptosis. PTEN/MMAC contains a PDZ domain-binding site, and we show here that the phosphatase binds to a PDZ domain ofmembrane-associated guanylate kinase with inverted orientation (MAGI) 3, a novel inverted membrane-associated guanylate kinase that localizes to epithelial cell tight junctions. Importantly, MAGI3 and PTEN/MMAC cooperate to modulate the kinase activity of AKT/PKB. These data suggest that MAGI3 allows for the juxtaposition of PTEN/MMAC to phospholipid signaling pathways involved with cell survival.

Donald Dowbenko - One of the best experts on this subject based on the ideXlab platform.

  • interaction of the tumor suppressor pten mmac with a pdz domain of magi3 a novel membrane associated guanylate kinase
    Journal of Biological Chemistry, 2000
    Co-Authors: Yan Wu, Susan D. Spencer, Richard P. Laura, Qimin Gu, Donald Dowbenko, Laurence A Lasky
    Abstract:

    Abstract PTEN/MMAC is a phosphatase that is mutated in multiple human tumors. PTEN/MMAC dephosphorylates 3-phosphorylated phosphatidylinositol phosphates that activate AKT/protein kinase B (PKB) kinase activity. AKT/PKB is implicated in the Inhibition of Apoptosis, and cell lines and tumors with mutated PTEN/MMAC show increased AKT/PKB kinase activity and resistance to Apoptosis. PTEN/MMAC contains a PDZ domain-binding site, and we show here that the phosphatase binds to a PDZ domain ofmembrane-associated guanylate kinase with inverted orientation (MAGI) 3, a novel inverted membrane-associated guanylate kinase that localizes to epithelial cell tight junctions. Importantly, MAGI3 and PTEN/MMAC cooperate to modulate the kinase activity of AKT/PKB. These data suggest that MAGI3 allows for the juxtaposition of PTEN/MMAC to phospholipid signaling pathways involved with cell survival.

  • Interaction of the Tumor Suppressor PTEN/MMAC with a PDZ Domain of MAGI3, a Novel Membrane-associated Guanylate Kinase
    Journal of Biological Chemistry, 2000
    Co-Authors: Yan Wu, Susan D. Spencer, Richard P. Laura, Qimin Gu, Donald Dowbenko, Laurence A Lasky
    Abstract:

    Abstract PTEN/MMAC is a phosphatase that is mutated in multiple human tumors. PTEN/MMAC dephosphorylates 3-phosphorylated phosphatidylinositol phosphates that activate AKT/protein kinase B (PKB) kinase activity. AKT/PKB is implicated in the Inhibition of Apoptosis, and cell lines and tumors with mutated PTEN/MMAC show increased AKT/PKB kinase activity and resistance to Apoptosis. PTEN/MMAC contains a PDZ domain-binding site, and we show here that the phosphatase binds to a PDZ domain ofmembrane-associated guanylate kinase with inverted orientation (MAGI) 3, a novel inverted membrane-associated guanylate kinase that localizes to epithelial cell tight junctions. Importantly, MAGI3 and PTEN/MMAC cooperate to modulate the kinase activity of AKT/PKB. These data suggest that MAGI3 allows for the juxtaposition of PTEN/MMAC to phospholipid signaling pathways involved with cell survival.

Susan D. Spencer - One of the best experts on this subject based on the ideXlab platform.

  • interaction of the tumor suppressor pten mmac with a pdz domain of magi3 a novel membrane associated guanylate kinase
    Journal of Biological Chemistry, 2000
    Co-Authors: Yan Wu, Susan D. Spencer, Richard P. Laura, Qimin Gu, Donald Dowbenko, Laurence A Lasky
    Abstract:

    Abstract PTEN/MMAC is a phosphatase that is mutated in multiple human tumors. PTEN/MMAC dephosphorylates 3-phosphorylated phosphatidylinositol phosphates that activate AKT/protein kinase B (PKB) kinase activity. AKT/PKB is implicated in the Inhibition of Apoptosis, and cell lines and tumors with mutated PTEN/MMAC show increased AKT/PKB kinase activity and resistance to Apoptosis. PTEN/MMAC contains a PDZ domain-binding site, and we show here that the phosphatase binds to a PDZ domain ofmembrane-associated guanylate kinase with inverted orientation (MAGI) 3, a novel inverted membrane-associated guanylate kinase that localizes to epithelial cell tight junctions. Importantly, MAGI3 and PTEN/MMAC cooperate to modulate the kinase activity of AKT/PKB. These data suggest that MAGI3 allows for the juxtaposition of PTEN/MMAC to phospholipid signaling pathways involved with cell survival.

  • Interaction of the Tumor Suppressor PTEN/MMAC with a PDZ Domain of MAGI3, a Novel Membrane-associated Guanylate Kinase
    Journal of Biological Chemistry, 2000
    Co-Authors: Yan Wu, Susan D. Spencer, Richard P. Laura, Qimin Gu, Donald Dowbenko, Laurence A Lasky
    Abstract:

    Abstract PTEN/MMAC is a phosphatase that is mutated in multiple human tumors. PTEN/MMAC dephosphorylates 3-phosphorylated phosphatidylinositol phosphates that activate AKT/protein kinase B (PKB) kinase activity. AKT/PKB is implicated in the Inhibition of Apoptosis, and cell lines and tumors with mutated PTEN/MMAC show increased AKT/PKB kinase activity and resistance to Apoptosis. PTEN/MMAC contains a PDZ domain-binding site, and we show here that the phosphatase binds to a PDZ domain ofmembrane-associated guanylate kinase with inverted orientation (MAGI) 3, a novel inverted membrane-associated guanylate kinase that localizes to epithelial cell tight junctions. Importantly, MAGI3 and PTEN/MMAC cooperate to modulate the kinase activity of AKT/PKB. These data suggest that MAGI3 allows for the juxtaposition of PTEN/MMAC to phospholipid signaling pathways involved with cell survival.