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      The Myxoma Poxvirus Protein, M11L, Prevents Apoptosis by Direct Interaction with the Mitochondrial Permeability Transition Pore

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          Abstract

          M11L, an antiapoptotic protein essential for the virulence of the myxoma poxvirus, is targeted to mitochondria and prevents the loss of mitochondrial membrane potential that accompanies cell death. In this study we show, using a cross-linking approach, that M11L physically associates with the mitochondrial peripheral benzodiazepine receptor (PBR) component of the permeability transition (PT) pore. Close association of M11L and the PBR is also indicated by fluorescence resonance energy transfer (FRET) analysis. Stable expression of M11L prevents the release of mitochondrial cytochrome c induced by staurosporine or protoporphyrin IX (PPIX), a ligand of the PBR. Transiently expressed M11L also prevents mitochondrial membrane potential loss induced by PPIX, or induced by staurosporine in combination with PK11195, another ligand of the PBR. Myxoma virus infection and the associated expression of early proteins, including M11L, protects cells from staurosporine- and Fas-mediated mitochondrial membrane potential loss and this effect is augmented by the presence of PBR. We conclude that M11L regulates the mitochondrial permeability transition pore complex, most likely by direct modulation of the PBR.

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          Most cited references 91

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          Mitochondrial control of cell death.

          In many instances, permeabilization of mitochondrial membranes is a rate-limiting step of apoptotic or necrotic cell demise. This has important consequences for the pathophysiology of cell death, as well as for its pharmacological control.
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            BCL-2 family members and the mitochondria in apoptosis.

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              The expanding role of mitochondria in apoptosis.

               X. Wang (2001)
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                Author and article information

                Journal
                J Exp Med
                The Journal of Experimental Medicine
                The Rockefeller University Press
                0022-1007
                1540-9538
                4 November 2002
                : 196
                : 9
                : 1127-1140
                Affiliations
                [1 ]Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G2H7, Canada
                [2 ]Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta T6G2S2, Canada
                [3 ]Department of Experimental Oncology, Cross Cancer Institute, University of Alberta, Edmonton, Alberta T6G1Z2, Canada
                [4 ]Department of Laboratory Medicine and Pathology, University of Alberta Hospital, Edmonton, Alberta T6G2B7, Canada
                [5 ]Department of Cell Biology, University of Alberta, Edmonton, Alberta T6G2H7, Canada
                [6 ]Department of Microbiology and Immunology, University of Western Ontario and The John P. Robarts Research Institute, London, Ontario N6G2V4, Canada
                Author notes

                Address correspondence to Dr. Grant McFadden, Department of Microbiology and Immunology, University of Western Ontario and The John P. Robarts Research Institute, London, Ontario N6G2V4, Canada. Phone: 519-663-3184; Fax: 519-663-3847; E-mail: mcfadden@ 123456robarts.ca

                Article
                20011247
                10.1084/jem.20011247
                2194110
                12417624
                Copyright © 2002, The Rockefeller University Press
                Categories
                Article

                Medicine

                apoptosis, poxviridae, mitochondria, pk11195, protoporphyrin ix

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