The BECN1 coiled coil domain: an "imperfect" homodimer interface that facilitates ATG14 and UVRAG binding.
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 coiled-coil 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.
Department of Applied Biology and Chemical Technology, State Key Laboratory of Chirosciences, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong, China.
Xiaohua
X
Li
Liqiang
L
He
Mingjie
M
Zhang
Zhenyu
Z
Yue
Yanxiang
Y
Zhao
D033942:Adaptor Proteins, Vesicular Transport / Q000378:metabolism*; D000818:Animals; D051017:Apoptosis Regulatory Proteins / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008954:Models, Biological; D011485:Protein Binding; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship; D025521:Tumor Suppressor Proteins / Q000378:metabolism*
D033942:Adaptor Proteins, Vesicular Transport; D051017:Apoptosis Regulatory Proteins; D025521:Tumor Suppressor Proteins