握住门把：hPMCA1/神经钙黏蛋白相互作用调节钙结合位点的可及性。
Hold the door: hPMCA1/neuroplastin interactions regulate Ca-binding site accessibility.
机构信息
Fels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, Philadelphia, PA, 19140, United States.
Fels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, Philadelphia, PA, 19140, United States; Department of Medical Genetics & Molecular Biochemistry, Temple University School of Medicine, Philadelphia, PA, 19140, United States.
出版信息
Cell Calcium. 2018 Dec;76:135-136. doi: 10.1016/j.ceca.2018.10.003. Epub 2018 Nov 1.
Abstract
In a September 2018 paper published in Nature Communications, Gong et al. identified the domains through which human PMCA1 and neuroplastin (NPTN) interact. Upon binding, hPMCA1 TM domains separate T110 in TM1 and A370 in TM3 to reveal the Ca-binding site. Thus, NPTN is able to directly modulate the accessibility of cytosolic Ca to PMCA.
摘要
在 2018 年 9 月发表于《自然通讯》的一篇论文中，龚等人确定了人类 PMCA1 和神经钙蛋白（NPTN）相互作用的结构域。结合后，hPMCA1 的跨膜结构域将 TM1 中的 T110 和 TM3 中的 A370 分开，暴露出钙结合位点。因此，NPTN 能够直接调节细胞质钙进入 PMCA 的可及性。
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本文引用的文献
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