Proteomics

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Proximity biotinylation of Expi293F cells stably expressing EGFR by EGFR-FabID

ABSTRACT: Expi293F cells stably expressing EGFR were treated with AGIA-FabID or EGFR-FabID in three biological replicates. Cell lysates were subjected to methanol-chloroform precipitation and digested with trypsin. Biotinylated peptides were purified by Tamavidin 2-REV and identified by LC-MS/MS analysis.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Hidetaka Kosako 

PROVIDER: PXD043525 | JPOST Repository | Tue Nov 14 00:00:00 GMT 2023

REPOSITORIES: jPOST

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109_Sawasaki_1_EGFR_stable_AGIA_FabID_Tama_FusionIT.raw Raw
111_Sawasaki_4_EGFR_stable_EGFR_FabID_Tama_FusionIT.raw Raw
113_Sawasaki_2_EGFR_stable_AGIA_FabID_Tama_FusionIT.raw Raw
115_Sawasaki_5_EGFR_stable_EGFR_FabID_Tama_FusionIT.raw Raw
117_Sawasaki_3_EGFR_stable_AGIA_FabID_Tama_FusionIT.raw Raw
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Publications

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

Yamada Kohdai K   Shioya Ryouhei R   Nishino Kohei K   Furihata Hirotake H   Hijikata Atsushi A   Kaneko Mika K MK   Kato Yukinari Y   Shirai Tsuyoshi T   Kosako Hidetaka H   Sawasaki Tatsuya T  

Nature communications 20231214 1

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 w  ...[more]

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