We are analyzing https://link.springer.com/article/10.1186/1471-2121-3-14.

Title:
Negative regulation of mitochondrial VDAC channels by C-Raf kinase | BMC Molecular and Cell Biology
Description:
Background Growth of cancer cells results from the disturbance of positive and negative growth control mechanisms and the prolonged survival of these genetically altered cells due to the failure of cellular suicide programs. Genetic and biochemical approaches have identified Raf family serine/threonine kinases B-Raf and C-Raf as major mediators of cell survival. C-Raf cooperates with Bcl-2/Bcl-XL in suppression of apoptosis by a mechanism that involves targeting of C-Raf to the outer mitochondrial membrane and inactivation of the pro-apoptotic protein Bad. However, apoptosis suppression by C-Raf also occurs in cells lacking expression of Bad or Bcl-2. Results Here we show that even in the absence of Bcl-2/Bcl-XL, mitochondria-targeted C-Raf inhibits cytochrome c release and caspase activation induced by growth factor withdrawal. To clarify the mechanism of Bcl-2 independent survival control by C-Raf at the mitochondria a search for novel mitochondrial targets was undertaken that identified voltage-dependent anion channel (VDAC), a mitochondrial protein (porin) involved in exchange of metabolites for oxidative phosphorylation. C-Raf forms a complex with VDAC in vivo and blocks reconstitution of VDAC channels in planar bilayer membranes in vitro. Conclusion We propose that this interaction may be responsible for the Raf-induced inhibition of cytochrome c release from mitochondria in growth factor starved cells. Moreover, C-Raf kinase-induced VDAC inhibition may regulate the metabolic function of mitochondria and mediate the switch to aerobic glycolysis that is common to cancer cells.
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Keywords {🔍}

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Topics {✒️}

human b-lymphocyte membrane-derived n-terminal amphipatic α-helix vander heiden mg voltage-dependent anion channel planar bilayer membranes pcdna3-encoding active mas-bxb ptracer-cmv-encoding ha-vdac1 150 ng/ml gst-c-rafdd transformation-deficient bcr/abl mutant gst-c-raf recombinant protein permeability transition pore mutant gst-c-rafdd protein lipid bilayer experiments expression plasmid pcdna3-mas-bxb gst-c-raf recombinant proteins phosphatidylinositol 3-kinase-dependent signals inactive gst-c-raf proteins pcdna3 encoding c-raf anti-apoptotic pak1 kinase gst-c-rafyy340/341dd positive control gst-c-raf rapp theodor-boveri-institut full size image constitutively active mas-bxb isopropyl-β-d-thiogalactopyranoside article download pdf yeast mutant temperature-sensitive pro-apoptotic protein bad recombinant gst-c-raf left-hand side arrow mas-bxb induced phosphorylation constitutively active c-raf c-raf inhibits apoptosis anti-c-raf antibody interleukin-3-dependent myeloid cells 3-mas-bxb k375w cells ha-tag fusion protein cooh-terminal transmembrane domain inhibits apoptotic mitochondrial cellular suicide programs inactive gst-c-raf active gst-c-rafdd active c-raf kinase phosphate-buffered saline solution inactive gst-c-rafk375w anti-c-raf antibodies raf induces nf-kappab c-raf kinase activity c-raf-vdac dimer gst-bcl-2δtm protein

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WebPage:
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         headline:Negative regulation of mitochondrial VDAC channels by C-Raf kinase
         description:Growth of cancer cells results from the disturbance of positive and negative growth control mechanisms and the prolonged survival of these genetically altered cells due to the failure of cellular suicide programs. Genetic and biochemical approaches have identified Raf family serine/threonine kinases B-Raf and C-Raf as major mediators of cell survival. C-Raf cooperates with Bcl-2/Bcl-XL in suppression of apoptosis by a mechanism that involves targeting of C-Raf to the outer mitochondrial membrane and inactivation of the pro-apoptotic protein Bad. However, apoptosis suppression by C-Raf also occurs in cells lacking expression of Bad or Bcl-2. Here we show that even in the absence of Bcl-2/Bcl-XL, mitochondria-targeted C-Raf inhibits cytochrome c release and caspase activation induced by growth factor withdrawal. To clarify the mechanism of Bcl-2 independent survival control by C-Raf at the mitochondria a search for novel mitochondrial targets was undertaken that identified voltage-dependent anion channel (VDAC), a mitochondrial protein (porin) involved in exchange of metabolites for oxidative phosphorylation. C-Raf forms a complex with VDAC in vivo and blocks reconstitution of VDAC channels in planar bilayer membranes in vitro. We propose that this interaction may be responsible for the Raf-induced inhibition of cytochrome c release from mitochondria in growth factor starved cells. Moreover, C-Raf kinase-induced VDAC inhibition may regulate the metabolic function of mitochondria and mediate the switch to aerobic glycolysis that is common to cancer cells.
         datePublished:2002-06-12T00:00:00Z
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            Outer Mitochondrial Membrane
            Permeability Transition Pore
            Planar Lipid Bilayer Membrane
            VDAC Channel
            Lipid Bilayer Experiment
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            Biological Microscopy
            Life Sciences
            general
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ScholarlyArticle:
      headline:Negative regulation of mitochondrial VDAC channels by C-Raf kinase
      description:Growth of cancer cells results from the disturbance of positive and negative growth control mechanisms and the prolonged survival of these genetically altered cells due to the failure of cellular suicide programs. Genetic and biochemical approaches have identified Raf family serine/threonine kinases B-Raf and C-Raf as major mediators of cell survival. C-Raf cooperates with Bcl-2/Bcl-XL in suppression of apoptosis by a mechanism that involves targeting of C-Raf to the outer mitochondrial membrane and inactivation of the pro-apoptotic protein Bad. However, apoptosis suppression by C-Raf also occurs in cells lacking expression of Bad or Bcl-2. Here we show that even in the absence of Bcl-2/Bcl-XL, mitochondria-targeted C-Raf inhibits cytochrome c release and caspase activation induced by growth factor withdrawal. To clarify the mechanism of Bcl-2 independent survival control by C-Raf at the mitochondria a search for novel mitochondrial targets was undertaken that identified voltage-dependent anion channel (VDAC), a mitochondrial protein (porin) involved in exchange of metabolites for oxidative phosphorylation. C-Raf forms a complex with VDAC in vivo and blocks reconstitution of VDAC channels in planar bilayer membranes in vitro. We propose that this interaction may be responsible for the Raf-induced inhibition of cytochrome c release from mitochondria in growth factor starved cells. Moreover, C-Raf kinase-induced VDAC inhibition may regulate the metabolic function of mitochondria and mediate the switch to aerobic glycolysis that is common to cancer cells.
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      pageStart:1
      pageEnd:12
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         Outer Mitochondrial Membrane
         Permeability Transition Pore
         Planar Lipid Bilayer Membrane
         VDAC Channel
         Lipid Bilayer Experiment
         Cell Biology
         Biological Microscopy
         Life Sciences
         general
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      name:Institut für Medizinische Strahlenkunde und Zellforschung (MSZ), Universität Würzburg, Würzburg, Germany
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      name:Institut für Medizinische Strahlenkunde und Zellforschung (MSZ), Universität Würzburg, Würzburg, Germany

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