NVL2 is a nucleolar AAA-ATPase that interacts with ribosomal protein L5 through its nucleolar localization sequence.

NVL2 is a nucleolar AAA-ATPase that interacts with ribosomal protein L5 through its nucleolar localization sequence.
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DOI:
10.1091/mbc.e04-08-0692
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发表时间:
2004-10
影响因子:
3.3
通讯作者:
M. Nagahama;Y. Hara;Akihiro Seki;Takeshi Yamazoe;Yumiko Kawate;T. Shinohara;K. Hatsuzawa;K. Tani-K.
M. Nagahama;Y. Hara;Akihiro Seki;Takeshi Yamazoe;Yumiko Kawate;T. Shinohara;K. Hatsuzawa;K. Tani-K.
中科院分区:
生物学3区
文献类型:
--
作者:
M. Nagahama;Y. Hara;Akihiro Seki;Takeshi Yamazoe;Yumiko Kawate;T. Shinohara;K. Hatsuzawa;K. Tani-K.

文献摘要

相似文献

NVL(核VCP样蛋白)是AAA-ATPase家族的成员之一,在哺乳动物细胞中以两种形式存在,其N末端延伸长度不同。在这里,我们发现它们在细胞核中的定位不同;NVL2主要存在于核仁中,而NVL1是核质。突变分析表明,NVL2中存在两个核定位信号,其中一个与NVL1相同。此外,在NVL2的N端额外区还发现了核仁定位信号。核仁定位信号是与核糖体蛋白L5相互作用的关键,在酵母双杂交筛选中,核糖体蛋白L5被鉴定为NVL2的特异性相互作用伙伴。NVL2与L5的相互作用是依赖于ATP的,可能参与了NVL2的核仁移位。这种相互作用的生理意义在于发现显性的负NVL2突变体抑制核糖体的生物合成,核糖体生物合成发生在核仁中。
NVL (nuclear VCP-like protein), a member of the AAA-ATPase family, is known to exist in two forms with N-terminal extensions of different lengths in mammalian cells. Here, we show that they are localized differently in the nucleus; NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Mutational analysis demonstrated the presence of two nuclear localization signals in NVL2, one of which is shared with NVL1. In addition, a nucleolar localization signal was found to exist in the N-terminal extra region of NVL2. The nucleolar localization signal is critical for interaction with ribosomal protein L5, which was identified as a specific interaction partner of NVL2 on yeast two-hybrid screening. The interaction of NVL2 with L5 is ATP-dependent and likely contributes to the nucleolar translocation of NVL2. The physiological implication of this interaction was suggested by the finding that a dominant negative NVL2 mutant inhibits ribosome biosynthesis, which is known to take place in the nucleolus.