Lipid Geometry and Bilayer Curvature Modulate LC3/GABARAP-Mediated Model Autophagosomal Elongation.

Biophysical Journal
Ane LandajuelaA Alonso

Abstract

Autophagy, an important catabolic pathway involved in a broad spectrum of human diseases, implies the formation of double-membrane-bound structures called autophagosomes (AP), which engulf material to be degraded in lytic compartments. How APs form, especially how the membrane expands and eventually closes upon itself, is an area of intense research. Ubiquitin-like ATG8 has been related to both membrane expansion and membrane fusion, but the underlying molecular mechanisms are poorly understood. Here, we used two minimal reconstituted systems (enzymatic and chemical conjugation) to compare the ability of human ATG8 homologs (LC3, GABARAP, and GATE-16) to mediate membrane fusion. We found that both enzymatically and chemically lipidated forms of GATE-16 and GABARAP proteins promote extensive membrane tethering and fusion, whereas lipidated LC3 does so to a much lesser extent. Moreover, we characterize the GATE-16/GABARAP-mediated membrane fusion as a phenomenon of full membrane fusion, independently demonstrating vesicle aggregation, intervesicular lipid mixing, and intervesicular mixing of aqueous content, in the absence of vesicular content leakage. Multiple fusion events give rise to large vesicles, as seen by cryo-electron m...Continue Reading

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Citations

Nov 17, 2017·Scientific Reports·Javier H HervásAlicia Alonso
May 12, 2018·Autophagy·Katarzyna Zientara-Rytter, Suresh Subramani
Aug 28, 2019·Cells·Alf Håkon Lystad, Anne Simonsen
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Jan 7, 2020·Current Opinion in Cell Biology·Noboru Mizushima
May 6, 2021·Cell Discovery·Sascha Martens, Dorotea Fracchiolla
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Aug 23, 2021·Biochimica Et Biophysica Acta. Biomembranes·Marina N IriondoAlicia Alonso

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