Abstract
Programmed cell death (apoptosis) is regulated by the Bcl-2 family of proteins. Although it remains unclear how these family members control apoptosis, they clearly have the capacity to regulate the permeability of intracellular membranes to ions and proteins. Proapoptotic members of the Bcl-2 family, especially Bax and Bid, have been extensively analyzed for the ability to form channels in membranes and to regulate preexisting channels. Anti-apoptotic members of the family tend to have the opposing effects on membrane channel formation. The molecular mechanisms of the different models for the permeabilization of membranes by the Bcl-2 family members and the regulation of Bcl-2 family member subcellular localizations are discussed.
MeSH terms
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Animals
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BH3 Interacting Domain Death Agonist Protein
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Carrier Proteins / physiology
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Intracellular Membranes / metabolism*
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Ion Channels / metabolism
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Membrane Lipids / metabolism
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Membrane Proteins / physiology
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Mitochondria / metabolism*
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Mitochondrial ADP, ATP Translocases / metabolism
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Mitochondrial Membrane Transport Proteins
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Mitochondrial Permeability Transition Pore
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Permeability
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Porins / metabolism
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Proto-Oncogene Proteins / antagonists & inhibitors
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Proto-Oncogene Proteins / metabolism
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Proto-Oncogene Proteins c-bcl-2 / physiology*
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Voltage-Dependent Anion Channels
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bcl-2 Homologous Antagonist-Killer Protein
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bcl-2-Associated X Protein
Substances
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BH3 Interacting Domain Death Agonist Protein
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Carrier Proteins
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Ion Channels
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Membrane Lipids
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Membrane Proteins
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Mitochondrial Membrane Transport Proteins
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Mitochondrial Permeability Transition Pore
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Porins
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Proto-Oncogene Proteins
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Proto-Oncogene Proteins c-bcl-2
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Voltage-Dependent Anion Channels
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bcl-2 Homologous Antagonist-Killer Protein
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bcl-2-Associated X Protein
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Mitochondrial ADP, ATP Translocases