Journal Article

FZJ-2015-06934

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Conformational Polymorphism in Autophagy-Related Protein GATE-16

Ma, P. ; Schillinger, O.FZJ* ; Schwarten, M.FZJ* ; Lecher, J.FZJ* ; Hartmann, R.FZJ* ; Stoldt, M.FZJ* ; Mohrlüder, J.FZJ* ; Olubiyi, O. ; Strodel, B.FZJ* ; Willbold, D.FZJ* ; Weiergräber, O. H. (Corresponding author)FZJ*

2015
American Chemical Society Columbus, Ohio

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Please use a persistent id in citations: doi:10.1021/acs.biochem.5b00366

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 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.

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 552 - Engineering Cell Function (POF3-552) (POF3-552)

Appears in the scientific report 2015

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Database coverage:
; BIOSIS Previews ; Current Contents - Life Sciences ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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