FRET detects lateral interaction between transmembrane domain of EGF receptor and ganglioside GM3 in lipid bilayers

Mikito Nakano, Shinya Hanashima*, Toshiaki Hara, Kazuya Kabayama, Yuya Asahina, Hironobu Hojo, Naoko Komura, Hiromune Ando, Thomas K.M. Nyholm, J. Peter Slotte, Michio Murata

*Corresponding author for this work

    Research output: Contribution to journalArticleScientificpeer-review

    9 Citations (Scopus)

    Abstract

    Ganglioside GM3 in the plasma membranes suppresses cell growth by preventing the autophosphorylation of the epidermal growth factor receptor (EGFR). Biological studies have suggested that GM3 interacts with the transmembrane segment of EGFR. Further biophysical experiments are particularly important for quantitative evaluation of the peptide-glycolipid interplay in bilayer membranes using a simple reconstituted system. To examine these interactions in this way, we synthesized the transmembrane segment of EGFR bearing a nitrobenzoxadiazole fluorophore (NBD-TM) at the N-terminus. The affinity between EGFR and GM3 was evaluated based on Förster resonance energy transfer (FRET) between NBD-TM and ATTO594-labeled GM3 in bilayers where their non-specific interaction due to lateral proximity was subtracted by using NBD-labeled phospholipid. This method for selectively detecting the specific lipid-peptide interactions in model lipid bilayers disclosed that the lateral interaction between GM3 and the transmembrane segment of EGFR plays a certain role in disturbing the formation of active EGFR dimers.

    Original languageEnglish
    Article number183623
    JournalBiochimica et Biophysica Acta - Biomembranes
    Volume1863
    Issue number8
    DOIs
    Publication statusPublished - 1 Aug 2021
    MoE publication typeA1 Journal article-refereed

    Keywords

    • EGF receptor
    • FRET
    • Ganglioside GM3
    • Lipid-peptide interaction
    • Transmembrane helix

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