An unusual arrangement of 13 zinc fingers in the vertebrate gene <i>Z13</i>

Schulz, Thomas C.; Hopwood, Blair; Rathjen, Peter D.; Wells, J. R. E.

doi:10.1042/bj3110219

Cited by 9 publications

(7 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Miz1 has an N-terminal POZ domain, which is required for its transcriptional activation and repression activity (28) and 13 zinc fingers (25)(26)(27). Miz1 localizes in both the cytoplasm and the nucleus (29).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Miz1 is a signal- and pathway-specific modulator or regulator (SMOR) that suppresses TNF-α-induced JNK1 activation

Liu

Zhao

Eilers

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

The proinflammatory cytokine TNF-␣ exerts its pleiotropic functions through activation of multiple downstream effectors, including JNK1. Yet, the underlying regulatory mechanism is incompletely understood. Here, we report that the transcription factor Myc-interacting zinc-finger protein 1 (Miz1) selectively suppresses TNF-␣-induced JNK1 activation and cell death independently of its transcription activity. Proteomics analysis and yeast two-hybrid screening reveal that Miz1 is a JNK-associated protein. The TNF-␣-induced activation of JNK1 is augmented in Miz1-deficient mouse embryonic fibroblasts (Miz1 ؊/؊ MEFs), but the augmentation is abrogated by reintroduction of Miz1 or its transcription-deficient mutant. The regulation by Miz1 is highly specific, because it regulates TNF-␣-induced TRAF2 K63-linked polyubiquitination. Neither JNK1 activation by IL-1␤ or UV nor TNF-␣-induced activation of p38, ERK, or IB kinase complex is affected by the loss of Miz1. The TNF-␣-induced cell death also is accelerated in Miz1 ؊/؊ MEFs. Upon TNF-␣ stimulation, Miz1 is degraded rapidly by the proteasome, relieving its suppression on JNK1 activation. Thus, our results show that in addition to being a transcription factor Miz1 acts as a signal-and pathway-specific modulator or regulator that specifically regulates TNF-␣-induced JNK1 activation and cell death.

show abstract

mentioning

confidence: 99%

“…Myc-interacting zinc-finger protein 1 (Miz1), also known as Z13, is member of the poxvirus and zinc-finger (POZ) domain/zincfinger transcription factor family (25)(26)(27). Miz1 has an N-terminal POZ domain, which is required for its transcriptional activation and repression activity (28) and 13 zinc fingers (25)(26)(27).…”

mentioning

confidence: 99%

Miz1 is a signal- and pathway-specific modulator or regulator (SMOR) that suppresses TNF-α-induced JNK1 activation

Liu

Zhao

Eilers

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…Nine of the zinc finger domains are clustered at the COOH terminus of the KS1 protein, whereas a 56-amino acid spacer separates an additional NH 2 -terminal zinc finger motif. In addition, a vestigial zinc finger, which is similar to the type previously described by Schulz et al (31) and to a vestigial zinc finger of another pancreatic protein (GenBank accession number U56862), is located within the 56-amino acid spacer region. Interestingly, KS1 also possesses consensus KRAB-A and KRAB-B motifs, highly conserved sequences which are present in approximately onethird of C 2 H 2 zinc finger proteins (19) (Fig.…”

Section: Molecular Characterization Of Ks1 a Novel Growth Factor-indmentioning

confidence: 83%

“…Identical amino acid residues of the consensus sequence are shaded. Note the vestigial zinc finger (VZF) of KS1 has several of the conserved amino acid residues of the consensus sequence but lacks a cysteine and histidine critical for coordinating a zinc ion (31). (b) Comparison of the KS1 KRAB-A and -B motifs with KRAB domains from other zinc finger proteins (14)(15)(16)19).…”

Section: Molecular Characterization Of Ks1 a Novel Growth Factor-indmentioning

confidence: 99%

KRAB-independent suppression of neoplastic cell growth by the novel zinc finger transcription factor KS1.

Gebelein¹,

Fernández-Zapico²,

Imoto³

et al. 1998

J. Clin. Invest.

View full text Add to dashboard Cite

The study of zinc finger proteins has revealed their potential to act as oncogenes or tumor suppressors. Here we report the molecular, biochemical, and functional characterization of KS1 (KRAB/zinc finger suppressor protein 1), a novel, ubiquitously expressed zinc finger gene initially isolated from a rat pancreas library. KS1 contains 10 C 2 H 2 zinc fingers, a KRAB-A/B motif, and an ID sequence that has been shown previously to participate in growth factor-regulated gene expression. Northern blot analysis using pancreatic cell lines demonstrates that KS1 mRNA is inducible by serum and epidermal growth factor, suggesting a role for this gene in cell growth regulation. Biochemical analysis reveals that KS1 is a nuclear protein containing two transcriptional repressor domains, R1 and R2. R1 corresponds to the KRAB-A motif, whereas R2 represents a novel sequence. Transformation assays using NIH3T3 cells demonstrate that KS1 suppresses transformation by the potent oncogenes Ha-ras, G ␣ 12, and G ␣

show abstract

“…Myc-interacting zinc-finger protein 1 (MIZ1), also known as zinc finger and BTB domain containing 17 (ZBTB17), is a member of the poxvirus and zinc-finger (POZ) domain/zincfinger transcription factor family [27][28][29]. It has 13 zinc fingers at its c-terminus and an N-terminal POZ domain, which is required for its transcriptional activity [29].…”

Section: Introductionmentioning

confidence: 99%

Myc-interacting zinc-finger protein 1 positively regulates Wnt signalling by protecting Dishevelled from Dapper1-mediated degradation

Huang

Wang

Chen

et al. 2015

Biochemical Journal

View full text Add to dashboard Cite

Wnt signalling regulates embryonic development and tissue homoeostasis by modulating cell proliferation, differentiation and migration. Dapper1 (Dpr1) has been shown to be an important key negative regulator of Wnt signalling by promoting Dishevelled (Dvl) degradation. In the present study, we found that Myc-interacting zinc-finger protein 1 (MIZ1) interacts with Dpr1 and this interaction attenuates the ability of Dpr1 to induce Dvl2 degradation, thus enhancing Wnt signalling. Mechanistically, MIZ1 is translocated from the nucleus to the cytoplasm upon Wnt3a stimulation or overexpression of Dpr1 and Dvl2, disrupting the interaction between Dpr1 and Dvl2. Furthermore, MIZ1 can promote the proliferation of breast cancer MDA-MB-231 and BT-549 cells through Wnt signalling and reverse the anti-proliferative effect of Dpr1 on colorectal cancer Caco-2. Together, our findings establish a novel layer of Wnt signalling regulation via the MIZ1-Dpr1-Dvl axis.

show abstract

An unusual arrangement of 13 zinc fingers in the vertebrate gene Z13

Cited by 9 publications

References 33 publications

Miz1 is a signal- and pathway-specific modulator or regulator (SMOR) that suppresses TNF-α-induced JNK1 activation

Miz1 is a signal- and pathway-specific modulator or regulator (SMOR) that suppresses TNF-α-induced JNK1 activation

KRAB-independent suppression of neoplastic cell growth by the novel zinc finger transcription factor KS1.

Myc-interacting zinc-finger protein 1 positively regulates Wnt signalling by protecting Dishevelled from Dapper1-mediated degradation

Contact Info

Product

Resources

About