Imperfect interface of Beclin1 coiled-coil domain regulates homodimer and heterodimer formation with Atg14L and UVRAG.
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ABSTRACT:
SUBMITTER: Li X
PROVIDER: S-EPMC3293417 | biostudies-literature | 2012 Feb
REPOSITORIES: biostudies-literature
Publications
Imperfect interface of Beclin1 coiled-coil domain regulates homodimer and heterodimer formation with Atg14L and UVRAG.
Li Xiaohua X He Liqiang L Che Ka Hing KH Funderburk Sarah F SF Pan Lifeng L Pan Nina N Zhang Mingjie M Yue Zhenyu Z Zhao Yanxiang Y
Nature communications 20120207
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 ...[more]
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