@article{433fdfc394404bb3ad493f0b632ee39d,
title = "The BECN1 coiled coil domain: An {"}imperfect{"} homodimer interface that facilitates ATG14 and UVRAG binding",
abstract = "The coiled-coil domain of BECN1 serves as a protein interaction platform to recruit two major autophagy regulators ATG14 and UVRAG. Our crystal structure of the BECN1 coiledcoil domain reveals a homodimer with an imperfect dimer interface. This {"}imperfect{"} feature favors the formation of a stable BECN1-ATG14 or BECN1- UVRAG heterodimer over a metastable BECN1 homodimer to promote autophagy and/or endocytic pathways.",
keywords = "ATG14, Autophagy, BECN1, Coiled-coil domain, UVRAG",
author = "Xiaohua Li and Liqiang He and Mingjie Zhang and Zhenyu Yue and Yanxiang Zhao",
note = "Funding Information: This work was supported by Hong Kong Research Grants Council grants PolyU5641/08M (Y.Z.), PolyU5640/ 11M (Y.Z.), HKUST6/CRF/10 (Y.Z. and M.Z.), CA07/08.SC01 (Y.Z. and M.Z.) and the National Institute of Health Grants R01NS060123–03 NIH/ NINDS (Z.Y.) and U54RR022220 NIH (Z.Y.). The authors declare no competing financial interests.",
year = "2012",
month = aug,
doi = "10.4161/auto.20750",
language = "English",
volume = "8",
pages = "1258--1260",
journal = "Autophagy",
issn = "1554-8627",
publisher = "Landes Bioscience",
number = "8",
}