Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/16415
Title: Imperfect interface of Beclin1 coiled-coil domain regulates homodimer and heterodimer formation with Atg14L and UVRAG
Authors: Li, X
He, L
Che, KH
Funderburk, SF
Pan, L
Pan, N
Zhang, M
Yue, Z
Zhao, Y 
Issue Date: 2012
Publisher: Nature Publishing Group
Source: Nature communications, 2012, v. 3, 662 How to cite?
Journal: Nature Communications 
Abstract: Beclin 1 is a core component of the Class III Phosphatidylinositol 3-Kinase VPS34 complex. The coiled coil domain of Beclin 1 serves as an interaction platform for assembly of distinct Atg14L-and UVRAG-containing complexes to modulate VPS34 activity. Here we report the crystal structure of the coiled coil domain that forms an antiparallel dimer and is rendered metastable by a series of 'imperfect' a-d' pairings at its coiled coil interface. Atg14L and UVRAG promote the transition of metastable homodimeric Beclin 1 to heterodimeric Beclin1-Atg14L/UVRAG assembly. Beclin 1 mutants with their 'imperfect' a-d' pairings modified to enhance self-interaction, show distinctively altered interactions with Atg14L or UVRAG. These results suggest that specific utilization of the dimer interface and modulation of the homodimer-heterodimer transition by Beclin 1-interacting partners may underlie the molecular mechanism that controls the formation of various Beclin1-VPS34 subcomplexes to exert their effect on an array of VPS34-related activities, including autophagy.
URI: http://hdl.handle.net/10397/16415
EISSN: 2041-1723
DOI: 10.1038/ncomms1648
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