WRNIP1 accumulates at laser light irradiated sites rapidly via its ubiquitin-binding zinc finger domain and independently from its ATPase domain

Hironoshin Nomura, Akari Yoshimura, Takato Edo, Shin Ichiro Kanno, Syusuke Tada, Masayuki Seki, Akira Yasui, Takemi Enomoto

    Research output: Contribution to journalArticlepeer-review

    9 Citations (Scopus)

    Abstract

    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.

    Original languageEnglish
    Pages (from-to)1145-1150
    Number of pages6
    JournalBiochemical and biophysical research communications
    Volume417
    Issue number4
    DOIs
    Publication statusPublished - 2012 Jan 27

    Keywords

    • ATPase
    • DNA damage
    • UBZ
    • Ubiquitin
    • WRNIP1

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology

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