LC3 and GATE-16 N termini mediate membrane fusion processes required for autophagosome biogenesis

Hilla Weidberg, Tomer Shpilka, Elena Shvets, Adi Abada, Frida Shimron, Zvulun Elazar

Research output: Contribution to journalArticlepeer-review

Abstract

Autophagy is a unique membrane trafficking pathway describing the formation and targeting of double membrane autophagosomes to the vacuole/lysosome. The biogenesis of autophagosomes and their delivery to the vacuole/lysosome depend on multiple membrane fusion events. Using a cell-free system, we have investigated the ability of LC3 and GATE-16, two mammalian Atg8 orthologs, to mediate membrane fusion. We found that both proteins promote tethering and membrane fusion, mediated by the proteins' N-terminal α helices. We further show that short, 10 amino acid long synthetic peptides derived from the N terminus of LC3 or GATE-16 are sufficient to promote membrane fusion. Our data indicate that the fusion activity of LC3 is mediated by positively charged amino acids, whereas the activity of GATE-16 is mediated by hydrophobic interactions. Finally, we demonstrate that LC3 and GATE-16 N termini in general and specific residues needed for the fusion activity are essential for the proteins role in autophagosome biogenesis.

Original languageEnglish
Pages (from-to)444-54
Number of pages11
JournalDevelopmental Cell
Volume20
Issue number4
DOIs
StatePublished - 19 Apr 2011

All Science Journal Classification (ASJC) codes

  • General Biochemistry,Genetics and Molecular Biology
  • Molecular Biology
  • Cell Biology
  • Developmental Biology

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