Evidence map›Paper›PMID 22261722›Full record

ArticleMolecular & cellular proteomics : MCP2012

Interaction proteomics identify NEURL4 and the HECT E3 ligase HERC2 as novel modulators of centrosome architecture.

Abdallah K Al-Hakim, Mikhail Bashkurov, Anne-Claude Gingras, Daniel Durocher, Laurence Pelletier

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

47 citing papers in PubMed, 71 citations in OpenAlex.

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  14. 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

5 authors at 3 institutions in 1 country.

Abdallah K Al-HakimSamuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario M5G 1X5, Canada.
Mikhail Bashkurov
Anne-Claude Gingras
Daniel Durocher
Laurence Pelletier
Mount Sinai Hospital · CALunenfeld-Tanenbaum Research Institute · CAUniversity of Toronto · CA

Funding

Canadian Institutes of Health Research MOP-84314
6 · The paper itself

Abstract

Centrosomes are composed of a centriole pair surrounded by an intricate proteinaceous matrix referred to as pericentriolar material. Although the mechanisms underpinning the control of centriole duplication are now well understood, we know relatively little about the control of centrosome size and shape. Here we used interaction proteomics to identify the E3 ligase HERC2 and the neuralized homologue NEURL4 as novel interaction partners of the centrosomal protein CP110. Using high resolution imaging, we find that HERC2 and NEURL4 localize to the centrosome and that interfering with their function alters centrosome morphology through the appearance of aberrant filamentous structures that stain for a subset of pericentriolar material proteins including pericentrin and CEP135. Using an RNA interference-resistant transgene approach in combination with structure-function analyses, we show that the association between CP110 and HERC2 depends on nonoverlapping regions of NEURL4. Whereas CP110 binding to NEURL4 is dispensable for the regulation of pericentriolar material architecture, its association with HERC2 is required to maintain normal centrosome integrity. NEURL4 is a substrate of HERC2, and together these results indicate that the NEURL4-HERC2 complex participates in the ubiquitin-dependent regulation of centrosome architecture.

Indexed as

Carrier ProteinsCell Cycle ProteinsCentrosomeChromatography, AffinityGene Knockdown TechniquesGuanine Nucleotide Exchange FactorsHEK293 CellsHumansMicrotubule-Associated ProteinsPhosphoproteinsProteasome Endopeptidase ComplexProtein Interaction MappingProtein Processing, Post-TranslationalProtein Structure, TertiaryProtein TransportProteomicsCarrier ProteinsCCP110 protein, humanCell Cycle ProteinsCEP97 protein, humanGuanine Nucleotide Exchange FactorsHERC2 protein, humanMicrotubule-Associated ProteinsNeurl4 protein, humanPhosphoproteinsProteasome Endopeptidase ComplexUbiquitin-Protein Ligases

Identifiers

PMID22261722
PMCPMC3433907
OpenAlexW2076455322

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.