Evidence map›Paper›PMID 10669742›Full record

ArticleMolecular and cellular biology2000

CIZ, a zinc finger protein that interacts with p130(cas) and activates the expression of matrix metalloproteinases.

T Nakamoto, T Yamagata, R Sakai, S Ogawa, H Honda, H Ueno, N Hirano, Y Yazaki, H Hirai

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.6field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

54 citing papers in PubMed, 133 citations in OpenAlex.

  1. Article
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  3. Review
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  8. Article
  9. Review
  10. Loss of the importiniScience · 2023
    Article
  11. Review
  12. Aquaporin-5 Dynamic Regulation.International journal of molecular sciences · 2023
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. p130Cas/Frontiers in cell and developmental biology · 2021
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

T NakamotoDepartment of Hematology and Oncology, Graduate School of Medicine, University of Tokyo, Hongo, Tokyo 113-8655, Japan.
T Yamagata
R Sakai
S Ogawa
H Honda
H Ueno
N Hirano
Y Yazaki
H Hirai
The University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

p130(cas) (Cas) is a docking protein that contains an SH3 domain and multiple tyrosine residues. p130(cas) is located at focal adhesions, is tyrosine phosphorylated in response to integrin stimulation, and is thought to transmit signals, via c-Crk and other proteins, for the remodeling of actin stress fibers and cell movement. In a search for the ligands of the SH3 domain of p130(cas) by far-Western screening, we cloned a novel protein named CIZ (for Cas-interacting zinc finger protein). CIZ consists of the following: a putative leucine zipper; a serine/threonine-rich region; a proline-rich sequence; five, six, or eight Krüppel-type C(2)H(2) zinc fingers; and the glutamine-alanine repeat. CIZ binds Cas in cells and is located in the nucleus and at focal adhesions. We showed that CIZ is a nucleocytoplasmic shuttling protein, by using the transient interspecies heterokaryon formation assay. In order to search for the targets of CIZ in nucleus, we determined the DNA binding consensus of CIZ as (G/C)AAAAA(A) by cyclic amplification and selection of targets analysis. The consensus-like sequences are found in several promoters of matrix metalloproteinases (MMPs), which are the enzymes used to degrade the extracellular matrix proteins. CIZ binds to a consensus-like sequence in the MMP-1 (collagenase) promoter. Overexpression of CIZ upregulates the transcriptions from MMP-1, MMP-3 (stromelysin), and MMP-7 (matrilysin) promoters, and this transactivation was enhanced in the presence of Cas. Furthermore, the stable overexpression of CIZ promoted the production of MMP-7 in culture medium. In summary, CIZ, a novel zinc finger protein, binds Cas, is a nucleocytoplasmic shuttling protein, and regulates the expression of MMPs.

Indexed as

Zinc FingersAmino Acid SequenceAnimalsBase SequenceCOS CellsCrk-Associated Substrate ProteinGene Expression Regulation, EnzymologicMatrix MetalloproteinasesMolecular Sequence DataNuclear Matrix-Associated ProteinsPhosphoproteinsProteinsRetinoblastoma-Like Protein p130Trans-ActivatorsTranscriptional ActivationTranscription FactorsCrk-Associated Substrate ProteinMatrix MetalloproteinasesNuclear Matrix-Associated ProteinsPhosphoproteinsProteinsRetinoblastoma-Like Protein p130Trans-ActivatorsTranscription FactorsZfp384 protein, rat

Identifiers

PMID10669742
PMCPMC85348
OpenAlexW2127571585

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.