8S1M

Crystal structure of human GABARAP fused to EGFR (1076-1099)

8S1M の概要

• エントリーDOI: 10.2210/pdb8s1m/pdb
• 分子名称: Epidermal growth factor receptor,Gamma-aminobutyric acid receptor-associated protein, CHLORIDE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: atg8, receptor-trafficking, protein binding
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17032.79

構造登録者

Ueffing, A.,Willbold, D.,Weiergraeber, O.H. (登録日: 2024-02-15, 公開日: 2024-08-14, 最終更新日: 2025-01-15)

主引用文献

Uffing, A.,Weiergraber, O.H.,Schwarten, M.,Hoffmann, S.,Willbold, D.
GABARAP interacts with EGFR - supporting the unique role of this hAtg8 protein during receptor trafficking.
Febs Lett., 598:2656-2669, 2024

PubMed 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.

PubMed: 39160442
DOI: 10.1002/1873-3468.14997

実験手法

X-RAY DIFFRACTION (2.05 Å)