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J Proteome Res. 2008 Dec;7(12):5333-8. doi: 10.1021/pr800498t.

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.

Author information

1
Center for Molecular Medicine, Section of Translational Neuropharmacology, Department of Physiology and Pharmacology, Karolinska Institute, 171 77 Stockholm, Sweden.

Abstract

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.

PMID:
19367709
DOI:
10.1021/pr800498t
[Indexed for MEDLINE]

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