Evidence map›Paper›PMID 25704760›Full record

ArticleExperimental cell research2015

Identification of the GTPase-activating protein DEP domain containing 1B (DEPDC1B) as a transcriptional target of Pitx2.

Di Wu, Xiaoxi Zhu, Kevin Jimenez-Cowell, Alexander J Mold, Christopher C Sollecito, Nicholas Lombana, Meng Jiao, Qize Wei

Abstract read
In one paragraph

Article in Experimental cell research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.3field-weighted citation impact, top 38% 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

10 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Article
  3. ERH Gene and Its Role in Cancer Cells.Frontiers in oncology · 2022
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
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

8 authors at 2 institutions in 2 countries.

Di WuDepartment of Biological Sciences, Fordham University, Bronx, NY 10458, United States.
Xiaoxi ZhuExperimental and Clinical Research Center (ECRC), a Cooperation between Max Delbrück Center and Charité Universitätsmedizin Berlin, Campus Buch, Berlin, Germany.
Kevin Jimenez-CowellDepartment of Biological Sciences, Fordham University, Bronx, NY 10458, United States.
Alexander J MoldDepartment of Biological Sciences, Fordham University, Bronx, NY 10458, United States.
Christopher C SollecitoDepartment of Biological Sciences, Fordham University, Bronx, NY 10458, United States.
Nicholas LombanaDepartment of Biological Sciences, Fordham University, Bronx, NY 10458, United States.
Meng JiaoDepartment of Biological Sciences, Fordham University, Bronx, NY 10458, United States.
Qize WeiDepartment of Biological Sciences, Fordham University, Bronx, NY 10458, United States. Electronic address: qwei3@fordham.edu.
Fordham University · USMax Delbrück Center · DE

Funding

Roles of MyoGEF in cytokinesisR15GM097702 · NIGMS · KANSAS STATE UNIVERSITY · PI WEI, QIZE · 2011 to 2015
$670k
Identification of downstream signals for Pitx2aK22HL071542 · NHLBI · KANSAS STATE UNIVERSITY · PI WEI, QIZE · 2005 to 2006
$357k
NHLBI NIH HHS K22 HL071542NIGMS NIH HHS R15 GM097702NIGMS NIH HHS R15GM097702
6 · The paper itself

Abstract

Pitx2 is a bicoid-related homeobox transcription factor implicated in regulating left-right patterning and organogenesis. However, only a limited number of Pitx2 downstream target genes have been identified and characterized. Here we demonstrate that Pitx2 is a transcriptional repressor of DEP domain containing 1B (DEPDC1B). The first intron of the human and mouse DEP domain containing 1B genes contains multiple consensus DNA-binding sites for Pitx2. Chromatin immunoprecipitation assays revealed that Pitx2, along with histone deacetylase 1, was recruited to the first intron of Depdc1b. In contrast, RNAi-mediated depletion of Pitx2 not only enhanced the acetylation of histone H4 in the first intron of Depdc1b, but also increased the protein level of Depdc1b. Luciferase reporter assays also showed that Pitx2 could repress the transcriptional activity mediated by the first intron of human DEPDC1B. The GAP domain of DEPDC1B interacted with nucleotide-bound forms of RAC1 in vitro. In addition, exogenous expression of DEPDC1B suppressed RAC1 activation and interfered with actin polymerization induced by the guanine nucleotide exchange factor TRIO. Moreover, DEPDC1B interacted with various signaling molecules such as U2af2, Erh, and Salm. We propose that Pitx2-mediated repression of Depdc1b expression contributes to the regulation of multiple molecular pathways, such as Rho GTPase signaling.

Indexed as

AnimalsBase SequenceBinding SitesEnzyme ActivationGTPase-Activating ProteinsHeLa CellsHomeobox Protein PITX2Homeodomain ProteinsHumansMiceNIH 3T3 CellsProtein BindingProtein Structure, Tertiaryrac1 GTP-Binding ProteinTranscriptional ActivationTranscription FactorsDEPDC1B protein, humanGTPase-Activating ProteinsHomeobox Protein PITX2Homeodomain Proteinsrac1 GTP-Binding ProteinRAC1 protein, humanTranscription FactorsDEPDC1BGTPase signalingPitx2Transcriptional regulation

Identifiers

PMID25704760
PMCPMC4387072
OpenAlexW2088053383

What OpenQuestion holds

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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.