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

Autophagy. 2012 Aug;8(8):1258-60. doi: 10.4161/auto.20750. Epub 2012 May 31.

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 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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Vesicular Transport / metabolism*
  • Animals
  • Apoptosis Regulatory Proteins / chemistry*
  • Apoptosis Regulatory Proteins / metabolism*
  • Humans
  • Models, Biological
  • Protein Binding
  • Protein Multimerization*
  • Protein Structure, Tertiary
  • Structure-Activity Relationship
  • Tumor Suppressor Proteins / metabolism*

Substances

  • Adaptor Proteins, Vesicular Transport
  • Apoptosis Regulatory Proteins
  • Tumor Suppressor Proteins