TY - JOUR
T1 - Cloning and characterization of a novel p21(Cip1/Waf1)-interacting zinc finger protein, Ciz1
AU - Mitsui, Kaoru
AU - Matsumoto, Akira
AU - Ohtsuka, Satoshi
AU - Ohtsubo, Motoaki
AU - Yoshimura, Akihiko
N1 - Funding Information:
We thank Ms. H. Ohgusu for excellent technical assistance and H. Toh for homology search. Part of this work was supported by grants from the Ministry of Science, Education, and Culture of Japan, the Uehara Memorial Foundation, the TORAY Research Foundation, the Naito Memorial Foundation, the Sumitomo Foundation, the No-vartis Foundation (Japan) for the Promotion of Science, the Mitsu-bishi Science foundation, and the Kanae Research Foundation. M.O. is supported by a fellowship from the Leukemia Society of America.
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 1999/10/22
Y1 - 1999/10/22
N2 - 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).
AB - 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).
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U2 - 10.1006/bbrc.1999.1516
DO - 10.1006/bbrc.1999.1516
M3 - Article
C2 - 10529385
AN - SCOPUS:0033595810
SN - 0006-291X
VL - 264
SP - 457
EP - 464
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -