Proximity extracellular protein-protein interaction analysis of EGFR using AirID-conjugated fragment of antigen binding

Kohdai Yamada, Ryouhei Shioya, Kohei Nishino, Hirotake Furihata, Atsushi Hijikata, Mika K. Kaneko, Yukinari Kato, Tsuyoshi Shirai, Hidetaka Kosako () and Tatsuya Sawasaki ()
Additional contact information
Kohdai Yamada: Ehime University
Ryouhei Shioya: Ehime University
Kohei Nishino: Tokushima University
Hirotake Furihata: Ehime University
Atsushi Hijikata: Tokyo University of Pharmacy and Life Sciences
Mika K. Kaneko: Tohoku University Graduate School of Medicine
Yukinari Kato: Tohoku University Graduate School of Medicine
Tsuyoshi Shirai: Nagahama Institute of BioScience and Technology
Hidetaka Kosako: Tokushima University
Tatsuya Sawasaki: Ehime University

Nature Communications, 2023, vol. 14, issue 1, 1-19

Abstract: Abstract Receptor proteins, such as epidermal growth factor receptor (EGFR), interact with other proteins in the extracellular region of the cell membrane to drive intracellular signalling. Therefore, analysis of extracellular protein-protein interactions (exPPIs) is important for understanding the biological function of receptor proteins. Here, we present an approach using a proximity biotinylation enzyme (AirID) fusion fragment of antigen binding (FabID) to analyse the proximity exPPIs of EGFR. AirID was C-terminally fused to the Fab fragment against EGFR (EGFR-FabID), which could then biotinylate the extracellular region of EGFR in several cell lines. Liquid Chromatography-Mass Spectrometry (LC-MS/MS) analysis indicated that many known EGFR interactors were identified as proximity exPPIs, along with many unknown candidate interactors, using EGFR-FabID. Interestingly, these proximity exPPIs were influenced by treatment with EGF ligand and its specific kinase inhibitor, gefitinib. These results indicate that FabID provides accurate proximity exPPI analysis of target receptor proteins on cell membranes with ligand and drug responses.

Date: 2023
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-023-43931-7 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-43931-7

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-023-43931-7

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().