PDZ Domain–Binding Motif Regulates Cardiomyocyte Compartment-Specific Na V 1.5 Channel Expression and Function | Zendy

Diana Shy | Zendy; Ludovic Gillet | Zendy; Jakob Ogrodnik | Zendy; Maxime Albesa | Zendy; Arie O. Verkerk | Zendy; Rianne Wolswinkel | Zendy; JeanSébastien Rougier | Zendy; Julien Barc | Zendy; Maria C. Essers | Zendy; Ninda Syam | Zendy; Roos F. Marsman | Zendy; Anneke M. van Mil | Zendy; Samuel Rotman | Zendy; Richard Redon | Zendy; Connie R. Bezzina | Zendy; Carol Ann Remme | Zendy; Hugues Abriel | Zendy

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PDZ Domain–Binding Motif Regulates Cardiomyocyte Compartment-Specific Na _V 1.5 Channel Expression and Function

Author(s) -

Diana Shy,

Ludovic Gillet,

Jakob Ogrodnik,

Maxime Albesa,

Arie O. Verkerk,

Rianne Wolswinkel,

JeanSébastien Rougier,

Julien Barc,

Maria C. Essers,

Ninda Syam,

Roos F. Marsman,

Anneke M. van Mil,

Samuel Rotman,

Richard Redon,

Connie R. Bezzina,

Carol Ann Remme,

Hugues Abriel

Publication year - 2014

Publication title -

circulation

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 7.795

H-Index - 607

eISSN - 1524-4539

pISSN - 0009-7322

DOI - 10.1161/circulationaha.113.007852

Subject(s) - pdz domain , medicine , microbiology and biotechnology , compartment (ship) , biology , geology , oceanography

Sodium channel NaV1.5 underlies cardiac excitability and conduction. The last 3 residues of NaV1.5 (Ser-Ile-Val) constitute a PDZ domain-binding motif that interacts with PDZ proteins such as syntrophins and SAP97 at different locations within the cardiomyocyte, thus defining distinct pools of NaV1.5 multiprotein complexes. Here, we explored the in vivo and clinical impact of this motif through characterization of mutant mice and genetic screening of patients.

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