Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2016 May 3;12(5):894-5.
doi: 10.1080/15548627.2016.1162364.

The Atg17-Atg31-Atg29 complex and Atg11 regulate autophagosome-vacuole fusion

Affiliations
Review

The Atg17-Atg31-Atg29 complex and Atg11 regulate autophagosome-vacuole fusion

Xu Liu et al. Autophagy. .

Abstract

The macroautophagy (hereafter autophagy) process involves de novo formation of double-membrane autophagosomes; after sequestering cytoplasm these transient organelles fuse with the vacuole/lysosome. Genetic studies in yeasts have characterized more than 40 autophagy-related (Atg) proteins required for autophagy, and the majority of these proteins play roles in autophagosome formation. The fusion of autophagosomes with the vacuole is mediated by the Rab GTPase Ypt7, its guanine nucleotide exchange factor Mon1-Ccz1, and soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins. However, these factors are not autophagosome-vacuole fusion specific. We recently showed that 2 autophagy scaffold proteins, the Atg17-Atg31-Atg29 complex and Atg11, regulate autophagosome-vacuole fusion by recruiting the vacuolar SNARE Vam7 to the phagophore assembly site (PAS), where an autophagosome forms in yeast.

Keywords: autophagy; fusion; lysosome; stress; vacuole.

PubMed Disclaimer

Comment on

  • doi: 10.1016/j.cub.2015.11.054

Similar articles

Cited by

Publication types

Substances

LinkOut - more resources