质膜Ca^2+-ATPase(PMCA)是P型ATPase家族的一员,在真核细胞中主要负责信号刺激后胞内高浓度Ca2+的清除扫尾工作,并对维持静息状态下较低Ca2+浓度起着重要的调节作用.PMCA的一级结构已被确定,拓扑学结构显示,它有10个跨膜区和3个胞浆功能区.它的4个编码基因可产生4种亚型(PMCA 1-4),这些亚型在功能与分布上存在差异.PMCA的活性可被钙调蛋白等多种因素调节,这与其结构特征息息相关.近年来,PMCA已被证实与脂筏结构有一定关联,它在信号传导和细胞凋亡中的作用也成为目前科学研究的焦点.本文主要对PMCA的结构、亚型和功能的研究现状进行综述.
Plasma membrane Ca^2+-ATPase(PMCA) belongs to the family of P-type ion transport ATPases and is involved in signal transduction and apoptosis.It is the sole carrier for high-affinity Ca^2+ extrusion found in eukaryotic cells,and plays critical roles in extruding cellular Ca^2+ after signalling events and in maintaining the low concentration of Ca^2+ in resting cells.The amino acid sequence of PMCA has been identified,while its three-dimensional structural data are not available yet.The predicted topological structures have shown that PMCA had ten transmembrane α helix that connected to the outside of the membranes.Most of the pump mass protruded into the cytoplasm with three main functional domains,containing sites for ATP hydrolysis,Ca^2+ binding and aspartyl phosphate formation.Four isoforms of PMCA(PMCA 1-4) are encoded by four genes,and exihibit different distributions and functions.The regulators of PMCA are often closely associated and share common characteristics in structures.PMCA can also be regulated by lipid rafts and caveolae.This review focuses on the studies of the structural-functional correlations of PMCA.