bi5b00366_si_001.pdf (3.4 MB)
Conformational Polymorphism in Autophagy-Related Protein GATE-16
journal contribution
posted on 2015-09-08, 00:00 authored by Peixiang Ma, Oliver Schillinger, Melanie Schwarten, Justin Lecher, Rudolf Hartmann, Matthias Stoldt, Jeannine Mohrlüder, Olujide Olubiyi, Birgit Strodel, Dieter Willbold, Oliver H. WeiergräberAutophagy 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.