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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 | Source: | Nature Communications, 7 2012, v. 3, no. , p. 1-11 | 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. | Publisher: | Nature Publishing Group | Journal: | Nature Communications | EISSN: | 2041-1723 | DOI: | 10.1038/ncomms1648 | Rights: | This work is licensed under a Creative Commons Attribution-NonCommercial-No Derivative Works 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/3.0/ © 2012 Macmillan Publishers Limited. All rights reserved. © 2012 Macmillan Publishers Limited. All rights reserved. The following publication Li, X., He, L., Che, K. et al. Imperfect interface of Beclin1 coiled-coil domain regulates homodimer and heterodimer formation with Atg14L and UVRAG. Nat Commun 3, 662 (2012) is available at https://dx.doi.org/10.1038/ncomms1648 |
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