Basic and editing mechanisms underlying ion transport and regulation in NCX variants.
作者： Daniel Khananshvili
DOI: 10.1016/J.CECA.2019.102131
关键词: Sodium-calcium exchanger 、 RNA splicing 、 Antiporters 、 Palmitoylation 、 Allosteric regulation 、 Chemistry 、 Ion transporter 、 Antiporter 、 Alternative splicing 、 Cell biology
摘要: Structure-dynamic analysis of archaeal NCX (NCX_Mj) provided new insights into the underlying mechanisms ion selectivity, ion-coupled alternating access, occlusion, and transport catalysis. This knowledge is relevant, not only for prokaryotic eukaryotic NCXs, but also other families belonging to superfamily Ca2+/CA antiporters. In parallel with mechanisms, structure-dynamic determinants regulatory CBD1 CBD2 domains have been resolved according which Ca2+-induced allosteric signal decoded at two-domain interface "secondarily" modified by a splicing segment CBD2. The exon-dependent combinations within control number Ca2+ binding sites (from zero three) CBD2, as well affinity off-rates both CBDs. specifically rigidify local segments CBDs, yielding Ca2+-dependent activation (through CBD1) alleviation Na+-induced inactivation CBD2). synergistic interactions between CBDs characteristically differ in NCX1 NCX3, thereby underscoring physiological relevance structure-controlled shaping ion-dependent regulation tissue-specific variants. How modules operate conjunction regulators (PIP2, palmitoylation, XIP, among others) an open question that remains be determined.
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