Evidence map›Paper›PMID 23964080›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2013

VBP1 facilitates proteasome and autophagy-mediated degradation of MutS homologue hMSH4.

Yang Xu, Chengtao Her

Open access · greenAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

16 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Prefoldin Function in Cellular Protein Homeostasis and Human Diseases.Frontiers in cell and developmental biology · 2021
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. DNA damage induced MutS homologue hMSH4 acetylation.International journal of molecular sciences · 2013
    Article
  16. 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

2 authors at 1 institution in 1 country.

Yang Xu1School of Molecular Biosciences, Mail Drop 64-7520, College of Veterinary Medicine, Washington State University, Pullman, WA 99164-7520, USA. cher@wsu.edu.
Chengtao Her
Washington State University · US

Funding

Roles of hMSH5 in DNA recombination and cellular response to anticancer treatmenR01GM084353 · NIGMS · WASHINGTON STATE UNIVERSITY · PI HER, CHENGTAO · 2010 to 2013
$1.1M
NIGMS NIH HHS GM084353NIGMS NIH HHS R01 GM084353
6 · The paper itself

Abstract

Ubiquitination is an important mechanism for the regulation of diverse cellular functions, including proteolysis and DNA repair. The human MutS family protein hMSH4 functions in meiotic recombinational DNA double-strand break (DSB) repair. It was previously observed that hMSH4 interacts with the von Hippel-Lindau binding protein 1 (VBP1), a partner of the VHL ubiquitin E3 ligase as well as a subunit of the prefoldin complex. In this study we address how ubiquitination regulates the homeostasis of hMSH4 in the human embryonic kidney cell line HEK293T. We demonstrate that VBP1 targets hMSH4 for degradation and identify a new VBP1 binding partner, p97, an AAA(+) ATPase involved in protein degradation and DNA damage response. VBP1, VHL, and p97 coexist in the hMSH4 immunocomplex and regulate the polyubiquitination of hMSH4. Furthermore, the results of this study demonstrate that VBP1 acts together with p97 to regulate hMSH4 degradation. Overall, this study has revealed a molecular mechanism by which VBP1 controls the levels of hMSH4 by ubiquitination in mitotic cells. Such a mechanism may be important for controlling the role of hMSH4 in regulating homologous recombination and nonhomologous DNA end joining-mediated DSB repair in human cells.

Indexed as

AutophagyProteolysisAdenosine TriphosphatasesCarrier ProteinsCell Cycle ProteinsCell Line, TumorCytoskeletal ProteinsHEK293 CellsHomeostasisHumansMolecular ChaperonesNuclear ProteinsProteasome Endopeptidase ComplexProtein BindingUbiquitinationAdenosine TriphosphatasesCarrier ProteinsCell Cycle ProteinsCytoskeletal ProteinsMolecular ChaperonesMSH4 protein, humanNuclear Proteinsp97 ATPaseProteasome Endopeptidase ComplexVBP1 protein, humanDSB repairp97ubiquitinationVHL

Identifiers

PMID23964080
PMCPMC3834780
OpenAlexW2010523686

What Socratic 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 Socratic graph.