1. Nat. Rev. Cardiol. doi:10.1038/nrcardio.2017.103
Figure 3 Distribution of structures in the intercalated disc of cardiomyocytes
Figure 3 | Distribution of structures in the intercalated disc of cardiomyocytes. a | Adherens junctions are combined with desmosomal proteins forming the area composita, which occupies the majority of the intercalated disc1. However, desmosomes also form separate plaques at the intercalated disc. b | Interactions between proteins from desmosomes and adherens junctions have been identified in the area composita (note catenin-β1 substitution by plakoglobin in adherens junctions66 and the plakophilin 2 [PKP2] interaction with catenin-α3 [αT]4). A functional gap junction is formed by cis and trans interaction of Cx43 forming the gap junction plaque. In the perinexus, Cx43 interacts with tight junction protein ZO-1 (ZO-1)73,74, which regulates the area of the gap junction, and with ankyrin-G (also known as ankyrin 3 or ANK3) and PKP2 (Refs 30,80), which limit the area of the perinexus. Note that connexin 43 (Cx43, also known as gap junction-α1 protein) also interacts with desmocollin 2 (DSC2; dashed arrow)76. The voltage-gated sodium-channel (VGSC) complex includes Nav1.5 and β subunits. Two clusters of VGSCs have been identified at the intercalated disc. One cluster associated with cadherin 2 in the area composita ('mini-nodes of Ranvier')18,91, and the other cluster located in the perinexus of the gap junction, where it interacts with Cx43 (Ref. 86) (dashed arrow) and the scaffolding proteins ankyrin-G and PKP2 to stabilize the complex30,80. The multiple interactions between structures at the intercalated disc support the concept of the connexome, although the location of the connexome in the intercalated disc is speculative. αE, catenin-α1; DES, desmin; DSG2, desmoglein 2; DSP, desmoplakin.
Moncayo-Arlandi, J. & Brugada, R. (2017) Unmasking the molecular link between arrhythmogenic cardiomyopathy and Brugada syndrome
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