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lüll The autophagy effector Beclin 1: a novel BH3-only protein Sinha S; Levine BOncogene 2008[Dec]; 27 Suppl 1 (Suppl 1): S137-48BH3 domains were originally discovered in the context of apoptosis regulators and they mediate binding of proapoptotic Bcl-2 family members to antiapoptotic Bcl-2 family members. Yet, recent studies indicate that BH3 domains do not function uniquely in apoptosis regulation; they also function in the regulation of another critical pathway involved in cellular and tissue homeostasis called autophagy. Antiapoptotic Bcl-2 homologs downregulate autophagy through interactions with the essential autophagy effector and haploinsufficient tumor suppressor, Beclin 1. Beclin 1 contains a BH3 domain, similar to that of Bcl-2 proteins, which is necessary and sufficient for binding to antiapoptotic Bcl-2 homologs and required for Bcl-2-mediated inhibition of autophagy. This review will summarize the evidence that the BH3 domain of Beclin 1 serves as a key structural motif that enables Bcl-2 to function not only as an antiapoptotic protein, but also as an antiautophagy protein.|Adaptor Proteins, Vesicular Transport/physiology[MESH]|Amino Acid Sequence[MESH]|Animals[MESH]|Apoptosis Regulatory Proteins/chemistry/genetics/*physiology[MESH]|Arabidopsis Proteins/physiology[MESH]|Autophagy/*physiology[MESH]|Beclin-1[MESH]|Conserved Sequence[MESH]|Eukaryotic Cells/cytology/metabolism[MESH]|Humans[MESH]|Membrane Proteins/chemistry/*physiology[MESH]|Mice[MESH]|Models, Molecular[MESH]|Molecular Sequence Data[MESH]|Protein Conformation[MESH]|Protein Interaction Mapping[MESH]|Protein Structure, Tertiary[MESH]|Proto-Oncogene Proteins c-bcl-2/metabolism[MESH]|Saccharomyces cerevisiae Proteins/physiology[MESH]|Sequence Alignment[MESH]|Sequence Homology, Amino Acid[MESH]|Signal Transduction/physiology[MESH]|Structure-Activity Relationship[MESH]|Tumor Suppressor Proteins/chemistry/physiology[MESH]|Vesicular Transport Proteins/physiology[MESH] |