This title appears in the Scientific Report :
2015
Please use the identifier:
http://dx.doi.org/10.1021/acs.biochem.5b00366 in citations.
Conformational Polymorphism in Autophagy-Related Protein GATE-16
Conformational Polymorphism in Autophagy-Related Protein GATE-16
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 conjugate...
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Personal Name(s): | Ma, Peixiang |
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Schillinger, Oliver / Schwarten, Melanie / Lecher, Justin / Hartmann, Rudolf / Stoldt, Matthias / Mohrlüder, Jeannine / Olubiyi, Olujide / Strodel, Birgit / Willbold, Dieter / Weiergräber, Oliver H. (Corresponding author) | |
Contributing Institute: |
Strukturbiochemie; ICS-6 |
Published in: | Biochemistry, 54 (2015) 35, S. 5469 - 5479 |
Imprint: |
Columbus, Ohio
American Chemical Society
2015
|
DOI: |
10.1021/acs.biochem.5b00366 |
PubMed ID: |
26284781 |
Document Type: |
Journal Article |
Research Program: |
Engineering Cell Function |
Publikationsportal JuSER |
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 Xray crystallography, nuclear magnetic resonance spectroscopy, and molecular dynamics simulations to study the conformational dynamics of Atg8-type proteins, using GATE-16 (Golgiassociated 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. |