A requirement for ER-derived COPII vesicles in phagophore initiation

Autophagy. 2014 Apr;10(4):708-9. doi: 10.4161/auto.28103. Epub 2014 Feb 12.

Abstract

A major unanswered question in the field of autophagy is how the double-membrane phagophore is formed. As this membrane expands, it engulfs proteins and organelles that are destined for degradation and then seals to form an autophagosome. A growing consensus in the field is that a subdomain of the ER initiates formation of the phagophore. We show that ER-derived COPII-coated vesicles, which bud from a specialized domain of the ER called the ER exit site (ERES), are a source of this membrane. This finding will now pave the way for a biochemical description of the early steps of phagophore initiation.

Keywords: Atg1; COPII; TRAPPIII; Ypt1; macroautophagy.

Publication types

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

MeSH terms

  • Autophagy / physiology*
  • COP-Coated Vesicles / metabolism*
  • Endoplasmic Reticulum / metabolism*
  • Membrane Proteins / metabolism*
  • Phagosomes / metabolism*
  • Proteolysis

Substances

  • Membrane Proteins