title: Why doesn't Beclin 1, a BH3-only protein, suppress the anti-apoptotic function of Bcl-2?
abstract: Beclin 1 binds to Bcl-2 through its BH3 domain and this interaction inhibits starvation-induced autophagy. However, we have found that when Beclin 1 binds thus to Bcl-2, it fails to inhibit Bcl-2-mediated protection against four different inducers of apoptosis. In this punctum, we discuss possible reasons why Beclin 1 fails to behave like other BH3-only proteins and induce apoptosis.
authors.affiliation: Laboratory of Transcription Regulation, Nencki Institute of Experimental Biology, Warsaw, Poland.
authors.forename: Iwona A
authors.initials: IA
authors.lastname: Ciechomska
authors.forename: Christoph G
authors.initials: CG
authors.lastname: Goemans
authors.forename: Aviva M
authors.initials: AM
authors.lastname: Tolkovsky
mesh_terms: D000818:Animals; D017209:Apoptosis; D051017:Apoptosis Regulatory Proteins / Q000378:metabolism*; D001343:Autophagy; D000071186:Beclin-1; D006367:HeLa Cells; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism*; D051379:Mice; D008954:Models, Biological; D019253:Proto-Oncogene Proteins c-bcl-2 / Q000378:metabolism*
chemical_list: D051017:Apoptosis Regulatory Proteins; C491997:BECN1 protein, human; D000071186:Beclin-1; D008565:Membrane Proteins; D019253:Proto-Oncogene Proteins c-bcl-2