Abstract:
:The Beclin 1 gene is a haplo-insufficient tumor suppressor and plays an essential role in autophagy. However, the molecular mechanism by which Beclin 1 functions remains largely unknown. Here we report the crystal structure of the evolutionarily conserved domain (ECD) of Beclin 1 at 1.6 Å resolution. Beclin 1 ECD exhibits a previously unreported fold, with three structural repeats arranged symmetrically around a central axis. Beclin 1 ECD defines a novel class of membrane-binding domain, with a strong preference for lipid membrane enriched with cardiolipin. The tip of a surface loop in Beclin 1 ECD, comprising three aromatic amino acids, acts as a hydrophobic finger to associate with lipid membrane, consequently resulting in the deformation of membrane and liposomes. Mutation of these aromatic residues rendered Beclin 1 unable to stably associate with lipid membrane in vitro and unable to fully rescue autophagy in Beclin 1-knockdown cells in vivo. These observations form an important framework for deciphering the biological functions of Beclin 1.
journal_name
Cell Resjournal_title
Cell researchauthors
Huang W,Choi W,Hu W,Mi N,Guo Q,Ma M,Liu M,Tian Y,Lu P,Wang FL,Deng H,Liu L,Gao N,Yu L,Shi Ydoi
10.1038/cr.2012.24subject
Has Abstractpub_date
2012-03-01 00:00:00pages
473-89issue
3eissn
1001-0602issn
1748-7838pii
cr201224journal_volume
22pub_type
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