Evidence map›Paper›PMID 20228063›Full record

ArticleThe Journal of biological chemistry2010

A novel C53/LZAP-interacting protein regulates stability of C53/LZAP and DDRGK domain-containing Protein 1 (DDRGK1) and modulates NF-kappaB signaling.

Jianchun Wu, Guohua Lei, Mei Mei, Yi Tang, Honglin Li

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

84 citing papers in PubMed, 125 citations in OpenAlex.

  1. Article
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  10. UFL1 promotes survival and function of virtual memory CD8 T cells.Journal of immunology (Baltimore, Md. : 1950) · 2025
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24 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Jianchun WuChildren's Memorial Research Center, Department of Pediatrics, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60614.
Guohua LeiChildren's Memorial Research Center, Department of Pediatrics, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60614.
Mei MeiChildren's Memorial Research Center, Department of Pediatrics, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60614.
Yi TangChildren's Memorial Research Center, Department of Pediatrics, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60614.
Honglin LiChildren's Memorial Research Center, Department of Pediatrics, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60614. Electronic address: h-li2@northwestern.edu.
Northwestern University · US

Funding

Functional study of C53 protein as a novel regulator of checkpoint kinasesR01GM081776 · NIGMS · LURIE CHILDREN'S HOSPITAL OF CHICAGO · PI LI, HONGLIN · 2008 to 2012
$1.5M
NIGMS NIH HHS R01 GM081776
6 · The paper itself

Abstract

C53/LZAP (also named as Cdk5rap3) is a putative tumor suppressor that plays important roles in multiple cell signaling pathways, including DNA damage response and NF-kappaB signaling. Yet how its function is regulated remains largely unclear. Here we report the isolation and characterization of two novel C53/LZAP-interacting proteins, RCAD (Regulator of C53/LZAP and DDRGK1) and DDRGK1 (DDRGK domain-containing protein 1). Our co-immunoprecipitation assays confirmed their interactions, while gel filtration assay indicated that C53/LZAP and RCAD may form a large protein complex. Intriguingly, we found that RCAD knockdown led to dramatic reduction of C53/LZAP and DDRGK1 proteins. We also found that C53/LZAP and DDRGK1 became more susceptible to the proteasome-mediated degradation in RCAD knockdown cells, whereas their ubiquitination was significantly attenuated by RCAD overexpression. In addition, we found that RCAD, like C53/LZAP, also plays an important role in regulation of NF-kappaB signaling and cell invasion. Taken together, our findings strongly suggest that RCAD is a novel regulator of C53/LZAP tumor suppressor and NF-kappaB signaling.

Indexed as

Base SequenceBlotting, NorthernCell Cycle ProteinsCell Line, TumorChromatography, GelDNA PrimersGene Knockdown TechniquesHumansIntracellular Signaling Peptides and ProteinsMicroscopy, ElectronNerve Tissue ProteinsNF-kappa BPolymerase Chain ReactionSignal TransductionTumor Suppressor ProteinsCDK5RAP3 protein, humanCell Cycle ProteinsDNA PrimersIntracellular Signaling Peptides and ProteinsNerve Tissue ProteinsNF-kappa BTumor Suppressor Proteins

Identifiers

PMID20228063
PMCPMC2865345
OpenAlexW1983374699

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.