ArticleOncogene2008
Monomeric but not trimeric clathrin heavy chain regulates p53-mediated transcription.
Article in Oncogene, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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.
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.
Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
- Abscisic acid enhances DNA damage response through the nuclear shuttling of clathrin light chain 2 in plant cells.Science advances · 2025Article
- Taming the Triskelion: Bacterial Manipulation of Clathrin.Microbiology and molecular biology reviews : MMBR · 2019Review
- Insufficiency of phosphatidylethanolamine N-methyltransferase is risk for lean non-alcoholic steatohepatitis.Scientific reports · 2016Article
- Clathrin Heavy Chain Interacts With Estrogen Receptor α and Modulates 17β-Estradiol Signaling.Molecular endocrinology (Baltimore, Md.) · 2015Article
- Unconventional functions for clathrin, ESCRTs, and other endocytic regulators in the cytoskeleton, cell cycle, nucleus, and beyond: links to human disease.Cold Spring Harbor perspectives in biology · 2014Review
- In silico docking, molecular dynamics and binding energy insights into the bolinaquinone-clathrin terminal domain binding site.Molecules (Basel, Switzerland) · 2014Article
- Analysis of flooding-responsive proteins localized in the nucleus of soybean root tips.Molecular biology reports · 2014Article
- Nuclear localization of clathrin involves a labile helix outside the trimerization domain.FEBS letters · 2013Article
- Endocytosis and signaling: cell logistics shape the eukaryotic cell plan.Physiological reviews · 2012Review
- Mitotic moonlighting functions for membrane trafficking proteins.Traffic (Copenhagen, Denmark) · 2011Review
- The endocytic matrix.Nature · 2010Review
- Functional characterization of the interactions between endosomal adaptor protein APPL1 and the NuRD co-repressor complex.The Biochemical journal · 2009Article
- Endocytic proteins in the regulation of nuclear signaling, transcription and tumorigenesis.Molecular oncology · 2009Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tumor suppressor p53 protein is the transcription factor responsible for various genes including DNA repair, growth arrest, apoptosis and antiangiogenesis. Recently, we showed that clathrin heavy chain (CHC), which was originally identified as a cytosolic protein regulating endocytosis, is present in nuclei and functions as a coactivator for p53. Here, we determined the detailed p53-binding site of CHC and a CHC deletion mutant containing this region (CHC833-1406) behaved as a monomer in cells. Monomeric CHC833-1406 still had a higher ability to transactivate p53 than wild-type CHC although this CHC mutant no longer had endocytic function. Moreover, similar to wild-type CHC, monomeric CHC enhances p53-mediated transcription through the recruitment of histone acetyltransferase p300. Immunofluorescent microscopic analysis exhibited that CHC833-1406 is predominantly localized in nuclei, suggesting that there may be a certain regulatory domain for nuclear export in the C-terminus of CHC. Thus, the trimerization domain of CHC is not necessary for the transactivation of p53 target genes and these data provide further evidence that nuclear CHC plays a role distinct from clathrin-mediated endocytosis.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.