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Dev Cell. 2011 Apr 19;20(4):444-54. doi: 10.1016/j.devcel.2011.02.006.

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

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  • 1Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel.

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.

Copyright © 2011 Elsevier Inc. All rights reserved.

PMID:
21497758
[PubMed - indexed for MEDLINE]
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