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@ARTICLE{ffing:1030471,
author = {Üffing, Alina and Weiergräber, Oliver H. and Schwarten,
Melanie and Hoffmann, Silke and Willbold, Dieter},
title = {{GABARAP} interacts with {EGFR} — supporting the unique
role of this h{A}tg8 protein during receptor trafficking},
journal = {FEBS letters},
volume = {x},
number = {x},
issn = {0014-5793},
address = {Chichester},
publisher = {Wiley},
reportid = {FZJ-2024-05317},
pages = {online ahead of print},
year = {2024},
abstract = {The human Atg8 family member GABARAP is involved in
numerous autophagy-related and -unrelated processes. We
recently observed that specifically the deficiency of
GABARAP enhances epidermal growth factor receptor (EGFR)
degradation upon ligand stimulation. Here, we report on two
putative LC3-interacting regions (LIRs) within EGFR, the
first of which (LIR1) is selected as a GABARAP binding site
in silico. Indeed, in vitro interaction studies reveal
preferential binding of LIR1 to GABARAP and GABARAPL1. Our
X-ray data demonstrate interaction of core LIR1 residues
FLPV with both hydrophobic pockets of GABARAP suggesting
canonical binding. Although LIR1 occupies the LIR docking
site, GABARAP Y49 and L50 appear dispensable in this case.
Our data support the hypothesis that GABARAP affects the
fate of EGFR at least in part through direct binding.},
cin = {IBI-7},
ddc = {610},
cid = {I:(DE-Juel1)IBI-7-20200312},
pnm = {5241 - Molecular Information Processing in Cellular Systems
(POF4-524) / SFB 1208 B02 - Spezifische Rollen von Atg8s im
Vesikeltransport (B02) (289554527)},
pid = {G:(DE-HGF)POF4-5241 / G:(GEPRIS)289554527},
typ = {PUB:(DE-HGF)16},
pubmed = {39160442},
UT = {WOS:001285593800001},
doi = {10.1002/1873-3468.14997},
url = {https://juser.fz-juelich.de/record/1030471},
}