14-3-3 Is a Regulator of the Cardiac Voltage-Gated Sodium
Channel Nav1.5
by Marie Allouis, Françoise Le Bouffant, Ronald Wilders, David Péroz, Jean-Jacques
Schott, Jacques Noireaud, Hervé Le Marec, Jean Mérot, Denis Escande, and
Isabelle Baró
Circulation Research
Volume 98(12):1538-1546
June 23, 2006
Copyright © American Heart Association, Inc. All rights reserved.
Figure 1. 14-3-3η associates with Nav1.5 first interdomain.
Marie Allouis et al. Circ Res. 2006;98:1538-1546
Copyright © American Heart Association, Inc. All rights reserved.
Figure 2. 14-3-3η associates with the 417 to 467 amino acid sequence of Nav1.5.
Marie Allouis et al. Circ Res. 2006;98:1538-1546
Copyright © American Heart Association, Inc. All rights reserved.
Figure 3. Nav1.5 ID I can interact with τ and ζ isoforms of 14-3-3.
Marie Allouis et al. Circ Res. 2006;98:1538-1546
Copyright © American Heart Association, Inc. All rights reserved.
Figure 4. Direct interaction of Nav1.5 and 14-3-3.
Marie Allouis et al. Circ Res. 2006;98:1538-1546
Copyright © American Heart Association, Inc. All rights reserved.
Figure 5. Colocalization of Nav1.5 and 14-3-3 in rabbit adult cardiomyocytes.
Marie Allouis et al. Circ Res. 2006;98:1538-1546
Copyright © American Heart Association, Inc. All rights reserved.
Figure 6. Functional effects of h14-3-3η on hNav1.5 channel in COS-7 cells.
Marie Allouis et al. Circ Res. 2006;98:1538-1546
Copyright © American Heart Association, Inc. All rights reserved.
Figure 7. A through C, Effects of the absence of the 14-3-3 protein on INa in simulated voltage
clamp experiments.
Marie Allouis et al. Circ Res. 2006;98:1538-1546
Copyright © American Heart Association, Inc. All rights reserved.
Figure 8. Simulated effects of the absence of the 14-3-3 protein on cardiac electrical restitution
properties.
Marie Allouis et al. Circ Res. 2006;98:1538-1546
Copyright © American Heart Association, Inc. All rights reserved.