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Updated: Apr 5, 2026

Study of Protein-protein Interactions in Autophagy Research
Published on: September 9, 2017
Conformational Polymorphism in Autophagy-Related Protein GATE-16
Peixiang Ma1,2, Oliver Schillinger1, Melanie Schwarten1
1Institute of Complex Systems, ICS-6 (Structural Biochemistry), Forschungszentrum Jülich , 52425 Jülich, Germany.
Abstract:
Autophagy is a fundamental homeostatic process in eukaryotic organisms, fulfilling essential roles in development and adaptation to stress. Among other factors, formation of autophagosomes critically depends on proteins of the Atg8 (autophagy-related protein 8) family, which are reversibly conjugated to membrane lipids. We have applied X-ray crystallography, nuclear magnetic resonance spectroscopy, and molecular dynamics simulations to study the conformational dynamics of Atg8-type proteins, using GATE-16 (Golgi-associated ATPase enhancer of 16 kDa), also known as GABARAPL2, as a model system. This combination of complementary approaches provides new insight into a structural transition centered on the C-terminus, which is crucial for the biological activity of these proteins.
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