Cloning and characterization of a novel p21(Cip1/Waf1)-interacting zinc finger protein, Ciz1

Kaoru Mitsui, Akira Matsumoto, Satoshi Ohtsuka, Motoaki Ohtsubo, Akihiko Yoshimura

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59 Citations (Scopus)


p21(Cip1/Waf1) inhibits cell-cycle progression by binding to G1 cyclin/CDK complexes and proliferating cell nuclear antigen (PCNA) through its N- and C-terminal domains, respectively. Here, we report a novel p21(Cip1/Waf1)-interacting protein, Ciz1 (for Cip1 interacting zinc finger protein), which contains polyglutamine repeats and glutamine-rich region in the N-terminus as well as three zinc-finger motifs and one MH3 (matrin 3-homologous domain 3) in the C-terminal region, Ciz1 bound to the N-terminal, the CDK2-interacting part of p21(Cip1/Waf1), and the interaction was disrupted by the overexpression of CDK2. A region of about 150 amino acids containing the first zinc-finger motif in Ciz1 was the binding site for p21(Cip/Waf1). When Ciz1 and p21(Cip/Waf1) were individually overexpressed in U2-OS cells, they mostly localized in the nucleus. However, coexpression of Ciz1 induced cytoplasmic distribution of p21(Cip1/Waf1). These data indicate that Ciz1 is a unique nuclear protein that regulates the cellular localization of p21(Cip/Waf1).

Original languageEnglish
Pages (from-to)457-464
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - 1999 Oct 22
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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