Post-translational regulation of cardiac Nav1.5 channels

Céline Marionneau

In this program, our objectives are :

• to identify novel phosphorylation and other post-translational modification sites on Na_v1.5 and its accessory/regulatory proteins using proteomic approaches performed from native cardiac tissues; and,
• to decipher the role of these sites in the post-translational regulation of Na_v1.5 channels by performing biochemical and electrophysiological analyses in freshly isolated cardiomyocytes genetically modified with adenoviruses.

• Proteomic analysis of native cerebellar iFGF14 complexes. Bosch MK, Nerbonne JM, Townsend RR, Miyazaki H, Nukina N, Ornitz DM, Marionneau C. Channels (Austin) 10: 297–312, 2016
• C-terminal phosphorylation of NaV1.5 impairs FGF13-dependent regulation of channel inactivation. Burel S, Coyan FC, Lorenzini M, Meyer MR, Lichti CF, Brown JH, Loussouarn G, Charpentier F, Nerbonne JM, Townsend RR, Maier LS, Marionneau C. J Biol Chem 292: 17431–17448, 2017.
• Regulation of the cardiac Na+ channel NaV1.5 by post-translational modifications. Marionneau C, Abriel H. J Mol Cell Cardiol 82: 36–47, 2015.
• Cardiac Sodium Current Under Sympathetic ControlProtein Phosphatase 2A Regulates Cardiac Na+ Channels.Marionneau C, Abriel H. Circ Res 124: 674–676, 2019.

Funding

• Agence Nationale de la Recherche : 2016-2020, ANR-DFG, Progress DHF, ANR-16-CE92-0013-01, with Lars Maier, University Hospital Regensburg, Germany, as co-principal investigator)
• Fondation d’entreprise Genavie : 2019-2020, Phosphoproteomic analysis of cardiac Na_v1.5 channels under β-adrenergic stimulation