Conformational Polymorphism in Autophagy-Related Protein GATE-16

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• 作者：Peixiang Ma ; Oliver Schillinger ; Melanie Schwarten ; Justin Lecher ; Rudolf Hartmann ; Matthias Stoldt ; Jeannine Mohrl眉der ; Olujide Olubiyi ; Birgit Strodel ; Dieter Willbold ; Oliver H. Weiergr盲ber
• 刊名：Biochemistry
• 出版年：2015
• 出版时间：September 8, 2015
• 年：2015
• 卷：54
• 期：35
• 页码：5469-5479
• 全文大小：514K
• ISSN：1520-4995

文摘

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.