Phospholipase Cδ1 associates with importin β1 and translocates into the nucleus in a Ca2+-dependent manner
Phospholipase Cδ1 associates with importin β1 and translocates into the nucleus in a Ca2+-dependent manner
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DOI：
10.1016/j.febslet.2005.07.082
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发表时间：
2005-09-12
期刊：
影响因子：
3.5
通讯作者：
Yagisawa, H
中科院分区：
文献类型：
--
作者：
Okada, M;Ishimoto, T;Yagisawa, H
磷脂酶C（PLC）delta（1）在细胞核和细胞质之间穿梭。在这里，我们证明了用离子霉素处理MDCK细胞和PC12细胞分别导致异位表达和内源性PLC delta（1）的核积累，这表明增加[Ca2+]（i）的信号触发核转位。为了阐明这种易位的分子机制，我们检测了PLC δ（1）是否与输入蛋白结合。PLC delta（1）在体外以Ca2+依赖性方式与importin beta 1相互作用，即使在没有importin alpha的情况下也是如此。缺乏与催化核心结合的Ca 2+的PLC delta（1）突变体E341A在任何生理Ca 2+浓度下都不显示这种相互作用，并且当在MDCK细胞中表达时，在离子霉素处理后没有易位到细胞核中。这些结果表明，PLC delta（1）的核输入是通过其与importin beta 1的Ca2+依赖性相互作用介导的。(c)2005年欧洲生物化学学会联合会。Elsevier B.V.出版，保留所有权利。
Phospholipase C (PLC)delta(1) shuttles between the nucleus and the cytoplasm. Here, we demonstrate that treatment of MDCK cells and PC12 cells with ionomycin causes nuclear accumulation of ectopically expressed and endogenous PLC delta(1), respectively, suggesting that signals that increase [Ca2+](i) trigger nuclear translocation. To clarify the molecular mechanisms involved in this translocation, we have examined whether PLC delta(1) binds with importins. PLC delta(1) interacted with importin beta 1 in a Ca2+-dependent manner in vitro even in the absence of importin alpha. A PLC delta(1) mutant E341A, which lacks Ca2+-binding to the catalytic core, did not show this interaction at any physiological Ca2+ concentration and did not translocate into the nucleus after ionomycin treatment when expressed in MDCK cells. These results suggested that the nuclear import of PLC delta(1) is mediated by its Ca2+-dependent interaction with importin beta 1. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.