钙调蛋白激活核蛋白导入：信号转导与核运输之间的联系。
Calmodulin activates nuclear protein import: a link between signal transduction and nuclear transport.
作者信息
Sweitzer T D, Hanover J A
机构信息
Laboratory of Cell Biochemistry and Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 26892-0850, USA.
出版信息
Proc Natl Acad Sci U S A. 1996 Dec 10;93(25):14574-9. doi: 10.1073/pnas.93.25.14574.
Abstract
In addition to the well-characterized GTP-dependent nuclear transport observed in permeabilized cells, we detected a mode of nuclear transport that was GTP-independent at elevated cytoplasmic calcium concentrations. Nuclear transport under these conditions was blocked by calmodulin inhibitors. Recombinant calmodulin restored ATP-dependent nuclear transport in the absence of cytosol. Calmodulin-dependent transport was inhibited by wheat germ agglutinin consistent with transport proceeding through nuclear pores. We propose that release of intracellular calcium stores upon cell activation inhibits GTP-dependent nuclear transport; the elevated cytosolic calcium then acts through calmodulin to stimulate the novel GTP-independent mode of import.
摘要
除了在通透细胞中观察到的特征明确的依赖GTP的核转运外，我们还检测到一种在细胞质钙浓度升高时不依赖GTP的核转运模式。在这些条件下的核转运被钙调蛋白抑制剂阻断。重组钙调蛋白在没有细胞质的情况下恢复了依赖ATP的核转运。依赖钙调蛋白的转运被麦胚凝集素抑制，这与通过核孔进行的转运一致。我们提出，细胞激活时细胞内钙库的释放会抑制依赖GTP的核转运；然后升高的细胞质钙通过钙调蛋白作用，以刺激新的不依赖GTP的输入模式。
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