SNARE proteins are required for macroautophagy

Usha Nair, Anjali Jotwani, Jiefei Geng, Gammoh Noor, Diana Richerson, Wei-Lien Yen, Janice Griffith, Shanta Nag, Ke Wang, Tyler Moss, Misuzu Baba, James A McNew, Xuejun Jiang, Fulvio Reggiori, Thomas J Melia, Daniel J Klionsky

Research output: Contribution to journalArticlepeer-review

Abstract

Macroautophagy mediates the degradation of long-lived proteins and organelles via the de novo formation of double-membrane autophagosomes that sequester cytoplasm and deliver it to the vacuole/lysosome; however, relatively little is known about autophagosome biogenesis. Atg8, a phosphatidylethanolamine-conjugated protein, was previously proposed to function in autophagosome membrane expansion, based on the observation that it mediates liposome tethering and hemifusion in vitro. We show here that with physiological concentrations of phosphatidylethanolamine, Atg8 does not act as a fusogen. Rather, we provide evidence for the involvement of exocytic Q/t-SNAREs in autophagosome formation, acting in the recruitment of key autophagy components to the site of autophagosome formation, and in regulating the organization of Atg9 into tubulovesicular clusters. Additionally, we found that the endosomal Q/t-SNARE Tlg2 and the R/v-SNAREs Sec22 and Ykt6 interact with Sso1-Sec9, and are required for normal Atg9 transport. Thus, multiple SNARE-mediated fusion events are likely to be involved in autophagosome biogenesis.
Original languageEnglish
Pages (from-to)290-302
Number of pages13
JournalCell
Volume146
Issue number2
DOIs
Publication statusPublished - 22 Jul 2011

Keywords

  • Autophagy
  • Liposomes
  • Membrane Proteins
  • Microtubule-Associated Proteins
  • Phagosomes
  • Phosphatidylethanolamines
  • Qa-SNARE Proteins
  • SNARE Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins

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