Use of surface plasmon resonance coupled with mass spectrometry reveals an interaction between the voltage-gated sodium channel type X alpha-subunit and caveolin-1.
The combination of surface plasmon resonance and mass spectrometry is emerging as a sensitive tool for the elucidation of protein-protein interactions. With the use of surface plasmon resonance-mass spectrometry, peptides, and brain extracts, we now report a novel interaction between the voltage-gated sodium channel type X alpha-subunit and caveolin-1, the central protein controlling caveolae formation. Surface plasmon resonance binding analyses show that this interaction involves amino acids 85-103 of voltage-gated sodium channel type X alpha-subunit and amino acids 81-100 of caveolin-1, a known scaffolding domain of caveolin-1. It is anticipated that the surface plasmon resonance-mass spectrometry approach utilized in this study will be important for the elucidation of protein-protein network analysis in native tissues including the brain.
Ohman
Elisabet
E
Center for Molecular Medicine, Section of Translational Neuropharmacology, Department of Physiology and Pharmacology, Karolinska Institute, 171 77 Stockholm, Sweden.
Nilsson
Anna
A
Madeira
Alexandra
A
Sjögren
Benita
B
Andrén
Per E
PE
Svenningsson
Per
P
D000818:Animals; D001921:Brain / Q000378:metabolism; D051242:Caveolin 1 / Q000378:metabolism*; D019295:Computational Biology; D006801:Humans; D007477:Ions; D008024:Ligands; D013058:Mass Spectrometry / Q000379:methods*; D021962:Membrane Microdomains / Q000378:metabolism; D051379:Mice; D062559:NAV1.8 Voltage-Gated Sodium Channel; D040081:Protein Array Analysis / Q000379:methods*; D025941:Protein Interaction Mapping; D051381:Rats; D015222:Sodium Channels / Q000378:metabolism*; D020349:Surface Plasmon Resonance / Q000379:methods*
D051242:Caveolin 1; D007477:Ions; D008024:Ligands; D062559:NAV1.8 Voltage-Gated Sodium Channel; C568317:SCN10A protein, human; C568318:Scn10a protein, mouse; C568319:Scn10a protein, rat; D015222:Sodium Channels