Assembly of Bcl-2 into microsomal and outer mitochondrial membranes

Bcl-2 is thought to associate spontaneously with membranes via a carboxyl-terminal hydrophobic domain by a mechanism analogous to that of cytochrome b5. We have examined the association of Bcl-2 with a variety of highly purified intracellular membranes in vitro. Fusion proteins were used to assess d...

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Veröffentlicht in:	The Journal of biological chemistry 1994-04, Vol.269 (13), p.9842-9849
Hauptverfasser:	JANIAK, F, LEBER, B, ANDREWS, D. W
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Animals, Newborn Biological and medical sciences Cell physiology Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes Cytochromes b5 - biosynthesis Cytochromes b5 - isolation & purification Dogs Fundamental and applied biological sciences. Psychology Intracellular Membranes - metabolism Liposomes Membrane Proteins - biosynthesis Membrane Proteins - isolation & purification Microsomes - metabolism Mitochondria, Heart - metabolism Mitochondria, Liver - metabolism Molecular and cellular biology Pancreas - metabolism Protein Biosynthesis Protein-Tyrosine Kinases - biosynthesis Proto-Oncogene Proteins - biosynthesis Proto-Oncogene Proteins - isolation & purification Proto-Oncogene Proteins c-bcl-2 Proto-Oncogenes Rats Rats, Sprague-Dawley Recombinant Fusion Proteins - biosynthesis Recombinant Fusion Proteins - isolation & purification Submitochondrial Particles - metabolism
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