Proteomic and functional mapping of cardiac NaV1.5 channel phosphorylation sites

URN to cite this document:: urn:nbn:de:bvb:355-epub-547877
DOI to cite this document:: 10.5283/epub.54787

Lorenzini, Maxime ; Burel, Sophie

; Lesage, Adrien

; Wagner, Emily

; Charrière, Camille

; Chevillard, Pierre-Marie ; Evrard, Bérangère ; Maloney, Dan ; Ruff, Kiersten M. ; Pappu, Rohit V.

; Wagner, Stefan

; Nerbonne, Jeanne M. ; Silva, Jonathan R. ; Townsend, R. Reid ; Maier, Lars S.

; Marionneau, Céline

License: Creative Commons Attribution Non-commercial Share Alike 4.0
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Date of publication of this fulltext: 05 Oct 2023 10:34

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Abstract

Phosphorylation of the voltage-gated Na+ (Na-V) channel Na(V)1.5 regulates cardiac excitability, yet the phosphorylation sites regulating its function and the underlying mechanisms remain largely unknown. Using a systematic, quantitative phosphoproteomic approach, we analyzed Na(V)1.5 channel complexes purified from nonfailing and failing mouse left ventricles, and we identified 42 ...