TY  - JOUR
AU  - Dobner, Jochen
AU  - Simons, Indra M.
AU  - Rufinatscha, Kerstin
AU  - Hänsch, Sebastian
AU  - Schwarten, Melanie
AU  - Weiergräber, Oliver H.
AU  - Abdollahzadeh, Iman
AU  - Gensch, Thomas
AU  - Bode, Johannes G.
AU  - Hoffmann, Silke
AU  - Willbold, Dieter
TI  - Deficiency of GABARAP but not its Paralogs Causes Enhanced EGF-induced EGFR Degradation
JO  - Cells
VL  - 9
IS  - 5
SN  - 2073-4409
CY  - Basel
PB  - MDPI
M1  - FZJ-2020-02051
SP  - 1296 -
PY  - 2020
AB  - The γ-aminobutyric acid type A receptor-associated protein (GABARAP) and its close paralogs GABARAPL1 and GABARAPL2 constitute a subfamily of the autophagy-related 8 (Atg8) protein family. Being associated with a variety of dynamic membranous structures of autophagic and non-autophagic origin, Atg8 proteins functionalize membranes by either serving as docking sites for other proteins or by acting as membrane tethers or adhesion factors. In this study, we describe that deficiency for GABARAP alone, but not for its close paralogs, is sufficient for accelerated EGF receptor (EGFR) degradation in response to EGF, which is accompanied by the downregulation of EGFR-mediated MAPK signaling, altered target gene expression, EGF uptake, and EGF vesicle composition over time. We further show that GABARAP and EGFR converge in the same distinct compartments at endogenous GABARAP expression levels in response to EGF stimulation. Furthermore, GABARAP associates with EGFR in living cells and binds to synthetic peptides that are derived from the EGFR cytoplasmic tail in vitro. Thus, our data strongly indicate a unique and novel role for GABARAP during EGFR trafficking.
LB  - PUB:(DE-HGF)16
C6  - pmid:32456010
UR  - <Go to ISI:>//WOS:000539340200230
DO  - DOI:10.3390/cells9051296
UR  - https://juser.fz-juelich.de/record/875459
ER  -