Key result
The organization of the Ca2+ binding domains (CBD1 and CBD2) plays an important role in the Ca2+ regulation of the Na+-Ca2+ exchanger.
This basic science study highlights the structural and functional importance of the organization of Ca2+ binding domains in regulating the Na+-Ca2+ exchanger in cardiomyocytes.
No immediate clinical implications for NCX modulation; extends molecular understanding of Ca2+ regulation in cardiomyocytes.
The Na(+)-Ca(2+) exchanger (NCX) is a plasma membrane protein particularly abundant in cardiomyocytes where it plays a prominent role in Ca(2+) extrusion. In addition to being transported, cytoplasmic Ca(2+) and Na(+) regulate NCX activity by activating and inhibiting ion transport, respectively. There are two Ca(2+) binding domains within the exchanger, CBD1 and CBD2, which have been crystallized and detailed structural information obtained. We have recently studied the roles of residues coordinating Ca(2+) in both CBD1 and CBD2. To gain further insight into NCX regulation, we investigate here the presence of possible functional interactions between the two CBDs. This study reveals the important role of CBD organization in Ca(2+) regulation of the exchanger.
No takes yet. Share an insight, caveat, or question.
Ottolia et al. (2010) studied this question. Ca2+ binding domains (CBD1 and CBD2) organization was evaluated on Functional interactions between CBD1 and CBD2. The organization of the Ca2+ binding domains (CBD1 and CBD2) plays an important role in the Ca2+ regulation of the Na+-Ca2+ exchanger.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: