The BECN1 coiled coil domain: An "imperfect" homodimer interface that facilitates ATG14 and UVRAG binding

Xiaohua Li, Liqiang He, Mingjie Zhang, Zhenyu Yue, Yanxiang Zhao

Research output: Contribution to journalShort surveypeer-review

3 Scopus citations

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.

Original languageEnglish
Pages (from-to)1258-1260
Number of pages3
JournalAutophagy
Volume8
Issue number8
DOIs
StatePublished - Aug 2012

Keywords

  • ATG14
  • Autophagy
  • BECN1
  • Coiled-coil domain
  • UVRAG

Fingerprint

Dive into the research topics of 'The BECN1 coiled coil domain: An "imperfect" homodimer interface that facilitates ATG14 and UVRAG binding'. Together they form a unique fingerprint.

Cite this