Apoptosis: mitochondrial membrane permeabilization--the (w)hole story?
One critical step of apoptosis is the release of mitochondrial proteins through the outer mitochondrial membrane. Recent work shows that two pro-apoptotic Bcl-2 family proteins, Bax and Bid, as well as the mitochondrion-specific lipid cardiolipin may cooperate in chemically defined liposomes to generate a protein-permeable conduit, relaunching the debate on the identity of the pore responsible for mitochondrial membrane permeabilization during apoptosis.
Zamzami
Naoufal
N
Centre National de la Recherche Scientifique, UMR1599, Institut Gustave Roussy, 39 rue Camille-Desmoulins, F-94805, Villejuif, France.
Kroemer
Guido
G
D000818:Animals; D017209:Apoptosis / Q000502:physiology*; D051023:BH3 Interacting Domain Death Agonist Protein; D002308:Cardiolipins / Q000378:metabolism; D002352:Carrier Proteins / Q000378:metabolism; D020169:Caspases / Q000378:metabolism; D066298:In Vitro Techniques; D007425:Intracellular Membranes / Q000378:metabolism; D020782:Matrix Metalloproteinases / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism*; D008954:Models, Biological; D010539:Permeability; D011518:Proto-Oncogene Proteins / Q000378:metabolism; D019253:Proto-Oncogene Proteins c-bcl-2; D051028:bcl-2-Associated X Protein
D051023:BH3 Interacting Domain Death Agonist Protein; D002308:Cardiolipins; D002352:Carrier Proteins; D011518:Proto-Oncogene Proteins; D019253:Proto-Oncogene Proteins c-bcl-2; D051028:bcl-2-Associated X Protein; D020169:Caspases; D020782:Matrix Metalloproteinases