Ciz1, Cip1 interacting zinc finger protein 1 binds the consensus DNA sequence ARYSR(0–2)YYAC

Warder, Daryl E.; Keherly, Michael J.

doi:10.1007/bf02256432

Cited by 41 publications

(65 citation statements)

References 27 publications

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“…Recently, it was reported that human Ciz1 does not colocalise with newly synthesized DNA (Warder and Keherly, 2003), which might appear to contradict our own observations. However, there were differences in the way the two studies were conducted.…”

Section: Sub-cellular Distribution Of Ciz1contrasting

confidence: 99%

“…Ciz1 has been implicated in tumorigenesis (Warder and Keherly, 2003) and has been linked to the mammalian cell cycle machinery, both by its interaction with p21…”

Section: Discussionmentioning

confidence: 99%

“…A potential role in transcription was proposed but not demonstrated, and no other function has been assigned to Ciz1. More recently the Ciz1 gene was isolated from a human medulloblastoma-derived cDNA library using an in vivo tumorigenesis model (Warder and Keherly, 2003). These two investigations used very different approaches to implicate Ciz1 in proliferation control in mammalian cells.…”

Section: Cip1mentioning

confidence: 99%

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Ciz1 promotes mammalian DNA replication

Coverley

Marr

Ainscough

2005

Journal of Cell Science

171

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Using a cell-free system that reconstitutes initiation of mammalian DNA replication, we identified a cyclin A-responsive protein, p21Cip1-interacting zinc finger protein 1 (Ciz1). In cell-free experiments, Ciz1 protein increases the number of nuclei that initiate DNA replication, and in intact cells GFP-tagged Ciz1 stimulates DNA synthesis, in both a wild-type and a p21Cip1 null background. Furthermore, mutation of a putative cyclin-dependent kinase phosphorylation site at threonines 191/2 alters Ciz1 activity in vitro, indicating that this site plays a role in regulating Ciz1. Consistent with a role in DNA replication, endogenous Ciz1 is present in nuclear foci that co-localize with PCNA during S phase, and targeted depletion of Ciz1 transcripts restrains cell proliferation by inhibiting entry to S phase. Ciz1-depleted cells accumulate with chromatin bound Mcm3 and PCNA but fail to synthesize DNA efficiently. These cell-based and cell-free experiments suggest that Ciz1 functions to promote DNA replication after replication complex formation. Finally, alternatively spliced forms of Ciz1 occur in embryonic cells from mouse and man, raising the possibility that Ciz1 splicing contributes to the regulation of DNA replication during development.

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Section: Sub-cellular Distribution Of Ciz1contrasting

confidence: 99%

“…Ciz1 has been implicated in tumorigenesis (Warder and Keherly, 2003) and has been linked to the mammalian cell cycle machinery, both by its interaction with p21…”

Section: Discussionmentioning

confidence: 99%

Section: Cip1mentioning

confidence: 99%

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Ciz1 promotes mammalian DNA replication

Coverley

Marr

Ainscough

2005

Journal of Cell Science

171

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“…The mechanism by which Ciz1 acts as a coactivator for ER is unclear at the moment. Because Ciz1 is known to interact with the DNA element (18) and because Ciz1 binds to the DNA-binding region of ER, we hypothesized that the DNA-binding activity of Ciz1 has an inherent role in ER-modifying activity. The DNA-binding motif of Ciz1 and its interaction with ER might create a better ER docking site on the DNA.…”

Section: Discussionmentioning

confidence: 99%

Ciz1, a Novel DNA-Binding Coactivator of the Estrogen Receptor α, Confers Hypersensitivity to Estrogen Action

et al. 2006

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The transcriptional activity of the estrogen receptor (ER) is affected by regulatory cofactors, including chromatinremodeling complexes, coactivators, and corepressors. Coregulators are recruited to target gene promoters through protein-protein interactions with ER and function as linker molecules between the DNA, DNA-binding proteins, and DNAmodifying enzymes. We recently showed that Cip-interacting zinc finger protein 1 (Ciz1) participates in the regulation of the cell cycle in estrogen-stimulated breast cancer cells. Despite the emerging significance of Ciz1 in the biology of breast cancer cells, regulation of endogenous Ciz1 in hormoneresponsive cancer cells remains unknown. To shed light on the role of Ciz1 in breast tumorigenesis, we defined the regulation of Ciz1 by the ER pathway and found that Ciz1 is an estrogen-responsive gene. We also discovered that Ciz1 protein, a DNA-binding factor, coregulates ER by enhancing ER transactivation activity by promoting the recruitment of the ER complex to the target gene chromatin. In addition, we found that Ciz1 overexpression confers estrogen hypersensitivity to breast cancer cells and promotes the growth rate, anchorage independency, and tumorigenic properties of breast cancer cells. These findings revealed the inherent role of Ciz1, a novel DNA binding and ER coactivator, in amplifying estrogenic responses and promoting breast cancer tumorigenesis.

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“…This approach has previously been utilized to determine specific DNA-binding sites for Ciz1 (Warder and Keherly 2003), the MT domain of MLL (Ayton et al 2004), and RAP1 (Graham and Chambers 1994), for example. A 72-bp oligonucleotide was synthesized, comprising a randomized 30-bp central region flanked by known sequences.…”

Section: Selected and Amplified Binding Assay (Saab)mentioning

confidence: 99%

High resolution structure of the HDGF PWWP domain: A potential DNA binding domain

Lukasik¹

2006

Protein Science

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Hepatoma Derived Growth Factor (HDGF) is an endogenous nuclear-targeted mitogen that is linked with human disease. HDGF is a member of the weakly conserved PWWP domain family. This 70-amino acid motif, originally identified from the WHSC1 gene, has been found in more than 60 eukaryotic proteins. In addition to the PWWP domain, many proteins in this class contain known chromatin remodeling domains, suggesting a role for HDGF in chromatin remodeling. We have determined the NMR structure of the HDGF PWWP domain to high resolution using a combination of NOEs, Jcouplings, and dipolar couplings. Comparison of this structure to a previously determined structure of the HDGF PWWP domain shows a significant difference in the C-terminal region. Comparison to structures of other PWWP domains shows a high degree of similarity to the PWWP domain structures from Dnmt3b and mHRP. The results of selected and amplified binding assay and NMR titrations with DNA suggest that the HDGF PWWP domain may function as a nonspecific DNA-binding domain. Based on the NMR titrations, we propose a model of the interaction of the PWWP domain with DNA.

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Ciz1, Cip1 interacting zinc finger protein 1 binds the consensus DNA sequence ARYSR(0–2)YYAC

Cited by 41 publications

References 27 publications

Ciz1 promotes mammalian DNA replication

Ciz1 promotes mammalian DNA replication

Ciz1, a Novel DNA-Binding Coactivator of the Estrogen Receptor α, Confers Hypersensitivity to Estrogen Action

High resolution structure of the HDGF PWWP domain: A potential DNA binding domain

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