WRNIP1 accumulates at laser light irradiated sites rapidly via its ubiquitin-binding zinc finger domain and independently from its ATPase domain.
WRNIP1 accumulates at laser light irradiated sites rapidly via its ubiquitin-binding zinc finger domain and independently from its ATPase domain.
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WRNIP1 通过其泛素结合锌指结构域在激光照射位点快速积累，并且独立于其 ATP 酶结构域。
DOI：
10.1016/j.bbrc.2011.12.080
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发表时间：
2012
期刊：
影响因子：
--
通讯作者：
T.
中科院分区：
文献类型：
--
作者：
Nomura;H.;Yoshimura;A.;Edo;T.;Kanno;S.I.;Tada;S.;Seki;M.;Yasui;A.;and Enomoto;T.
WRNIP1(Werner Helicase-Interaction Protein 1)最初被鉴定为一种与Werner综合征相关基因产物相互作用的蛋白质。WRNIP1在N-末端含有一个泛素结合锌指(UBZ)结构域，在C-末端含有两个亮氨酸拉链基序。此外，它在分子中间有一个ATPase结构域，赖氨酸残基在整个分子中作为泛素受体。在这里，我们报道了WRNIP1通过其泛素结合的锌指结构域在激光照射的部位非常迅速地聚集，已知该结构域结合了多泛素并参与了WRNIP1本身的泛素化。WRNIP1在激光照射部位的积累还需要包含两个亮氨酸拉链的C-末端区域，据报道这参与了WRNIP1的齐聚。突变的WRNIP1的ATPase结构域缺失或赖氨酸残基突变作为泛素受体，在激光照射的部位积累，这表明WRNIP1的ATPase结构域和WRNIP1的泛素化是积累所必需的。
WRNIP1 (Werner helicase-interacting protein 1) was originally identified as a protein that interacts with the Werner syndrome responsible gene product. WRNIP1 contains a ubiquitin-binding zinc-finger (UBZ) domain in the N-terminal region and two leucine zipper motifs in the C-terminal region. In addition, it possesses an ATPase domain in the middle of the molecule and the lysine residues serving as ubiquitin acceptors in the entire of the molecule. Here, we report that WRNIP1 accumulates in laser light irradiated sites very rapidly via its ubiquitin-binding zinc finger domain, which is known to bind polyubiquitin and to be involved in ubiquitination of WRNIP1 itself. The accumulation of WRNIP1 in laser light irradiated sites also required the C-terminal region containing two leucine zippers, which is reportedly involved in the oligomerization of WRNIP1. Mutated WRNIP1 with a deleted ATPase domain or with mutations in lysine residues, which serve as ubiquitin acceptors, accumulated in laser light irradiated sites, suggesting that the ATPase domain of WRNIP1 and ubiquitination of WRNIP1 are dispensable for the accumulation.