Journal Article FZJ-2024-05317

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GABARAP interacts with EGFR — supporting the unique role of this hAtg8 protein during receptor trafficking

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2024
Wiley Chichester

FEBS letters x(x), online ahead of print () [10.1002/1873-3468.14997]

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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.

Classification:

Contributing Institute(s):
  1. Strukturbiochemie (IBI-7)
Research Program(s):
  1. 5241 - Molecular Information Processing in Cellular Systems (POF4-524) (POF4-524)
  2. SFB 1208 B02 - Spezifische Rollen von Atg8s im Vesikeltransport (B02) (289554527) (289554527)

Appears in the scientific report 2024
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Medline ; Creative Commons Attribution CC BY 4.0 ; OpenAccess ; BIOSIS Previews ; Biological Abstracts ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; DEAL Wiley ; Ebsco Academic Search ; Essential Science Indicators ; IF < 5 ; JCR ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection
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 Record created 2024-08-30, last modified 2025-02-03


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