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@ARTICLE{Ma:276569,
author = {Ma, Peixiang and Schillinger, Oliver and Schwarten, Melanie
and Lecher, Justin and Hartmann, Rudolf and Stoldt, Matthias
and Mohrlüder, Jeannine and Olubiyi, Olujide and Strodel,
Birgit and Willbold, Dieter and Weiergräber, Oliver H.},
title = {{C}onformational {P}olymorphism in {A}utophagy-{R}elated
{P}rotein {GATE}-16},
journal = {Biochemistry},
volume = {54},
number = {35},
issn = {1520-4995},
address = {Columbus, Ohio},
publisher = {American Chemical Society},
reportid = {FZJ-2015-06934},
pages = {5469 - 5479},
year = {2015},
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.},
cin = {ICS-6},
ddc = {570},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {552 - Engineering Cell Function (POF3-552)},
pid = {G:(DE-HGF)POF3-552},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000361086500009},
pubmed = {pmid:26284781},
doi = {10.1021/acs.biochem.5b00366},
url = {https://juser.fz-juelich.de/record/276569},
}