Evidence map›Paper›PMID 25476789›Full record

ArticleJournal of proteome research2015

Proteomic analysis and identification of cellular interactors of the giant ubiquitin ligase HERC2.

Jeffrey T Galligan, Gustavo Martinez-Noël, Verena Arndt, Sebastian Hayes, Thomas W Chittenden, J Wade Harper, Peter M Howley

Open access · bronzeAbstract read
In one paragraph

Article in Journal of proteome research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

37 citing papers in PubMed, 59 citations in OpenAlex.

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  7. 1-L Transcription of SARS-CoV-2 Spike Protein S1 Subunit.International journal of molecular sciences · 2024
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  8. Article
  9. Review
  10. Regulation of MAPK Signaling Pathways by the Large HERC Ubiquitin Ligases.International journal of molecular sciences · 2023
    Review
  11. Article
  12. Review
  13. Stem cell models of Angelman syndrome.Frontiers in cell and developmental biology · 2023
    Review
  14. Article
  15. Article
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  18. Novel loss-of-function mutation inJournal of medical genetics · 2021
    Article
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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

7 authors at 1 institution in 1 country.

Jeffrey T GalliganDepartment of Microbiology and Immunobiology, Harvard Medical School , 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, United States.
Gustavo Martinez-Noël
Verena Arndt
Sebastian Hayes
Thomas W Chittenden
J Wade Harper
Peter M Howley
Harvard University · US

Funding

VIRAL ONCOPROTEIN PERTURBATION OF RB/E2F PATHWAYP01CA050661 · NCI · DANA-FARBER CANCER INSTITUTE · PI HOWLEY, PETER M · 1989 to 2013
$35.8M
MOLECULAR BASIS OF VIRAL INFECTIVITYT32AI007245 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI Aaron Gregory Schmidt · 1985 to 2026
$11.3M
Ubiquitin Mediated Proteolysis and Cell Cycle ControlR01AG011085 · NIA · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI JEFFREY W HARPER · 1993 to 2026
$10.9M
NCI NIH HHS P01CA50661NIAID NIH HHS T32 AI007245NIAID NIH HHS T32AI007245NIA NIH HHS R01 AG011085NIA NIH HHS R01AG011085
6 · The paper itself

Abstract

HERC2 is a large E3 ubiquitin ligase with multiple structural domains that has been implicated in an array of cellular processes. Mutations in HERC2 are linked to developmental delays and impairment caused by nervous system dysfunction, such as Angelman Syndrome and autism-spectrum disorders. However, HERC2 cellular activity and regulation remain poorly understood. We used a broad proteomic approach to survey the landscape of cellular proteins that interact with HERC2. We identified nearly 300 potential interactors, a subset of which we validated binding to HERC2. The potential HERC2 interactors included the eukaryotic translation initiation factor 3 complex, the intracellular transport COPI coatomer complex, the glycogen regulator phosphorylase kinase, beta-catenin, PI3 kinase, and proteins involved in fatty acid transport and iron homeostasis. Through a complex bioinformatic analysis of potential interactors, we linked HERC2 to cellular processes including intracellular protein trafficking and transport, metabolism of cellular energy, and protein translation. Given its size, multidomain structure, and association with various cellular activities, HERC2 may function as a scaffold to integrate protein complexes and bridge critical cellular pathways. This work provides a significant resource with which to interrogate HERC2 function more deeply and evaluate its contributions to mechanisms governing cellular homeostasis and disease.

Indexed as

Guanine Nucleotide Exchange FactorsHumansProtein Interaction MappingProteinsProteomeProteomicsUbiquitin-Protein LigasesGuanine Nucleotide Exchange FactorsHERC2 protein, humanProteinsProteomeUbiquitin-Protein Ligasescellular energy metabolismeIF3HERC2intracellular transporttranslationtranslational initiationUBE3A (E6AP)vesicle-mediated transport

Identifiers

PMID25476789
PMCPMC4324439
OpenAlexW2059562354

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.