Evidence map›Paper›PMID 32086376›Full record

ArticleThe Journal of biological chemistry2020

The ubiquitin ligase FBXW7 targets the centriolar assembly protein HsSAS-6 for degradation and thereby regulates centriole duplication.

Binshad Badarudeen, Ria Gupta, Sreeja V Nair, Aneesh Chandrasekharan, Tapas K Manna

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.8field-weighted citation impact, top 33% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. The E3 ligase Poe promotes Pericentrin degradation.Molecular biology of the cell · 2023
    Article
  4. Review
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 2 institutions in 1 country.

Binshad BadarudeenSchool of Biology, Indian Institute of Science Education and Research, Thiruvananthapuram, Vithura, Thiruvananthapuram 695551, Kerala, India.ORCID 0000-0002-8234-5912
Ria GuptaSchool of Biology, Indian Institute of Science Education and Research, Thiruvananthapuram, Vithura, Thiruvananthapuram 695551, Kerala, India.
Sreeja V NairSchool of Biology, Indian Institute of Science Education and Research, Thiruvananthapuram, Vithura, Thiruvananthapuram 695551, Kerala, India.
Aneesh ChandrasekharanRajiv Gandhi Centre for Biotechnology, Thiruvananthapuram 695014, Kerala, India.
Tapas K MannaSchool of Biology, Indian Institute of Science Education and Research, Thiruvananthapuram, Vithura, Thiruvananthapuram 695551, Kerala, India tmanna@iisertvm.ac.in.ORCID 0000-0002-2213-6246
Indian Institute of Science Education and Research Thiruvananthapuram · INRajiv Gandhi Centre for Biotechnology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Formation of a single new centriole from a pre-existing centriole is strictly controlled to maintain correct centrosome number and spindle polarity in cells. However, the mechanisms that govern this process are incompletely understood. Here, using several human cell lines, immunofluorescence and structured illumination microscopy methods, and ubiquitination assays, we show that the E3 ubiquitin ligase F-box and WD repeat domain-containing 7 (FBXW7), a subunit of the SCF ubiquitin ligase, down-regulates spindle assembly 6 homolog (HsSAS-6), a key protein required for procentriole cartwheel assembly, and thereby regulates centriole duplication. We found that FBXW7 abrogation stabilizes HsSAS-6 and increases its recruitment to the mother centriole at multiple sites, leading to supernumerary centrioles. Ultrastructural analyses revealed that FBXW7 is broadly localized on the mother centriole and that its presence is reduced at the site where the HsSAS-6-containing procentriole is formed. This observation suggested that FBXW7 restricts procentriole assembly to a specific site to generate a single new centriole. In contrast, during HsSAS-6 overexpression, FBXW7 strongly associated with HsSAS-6 at the centriole. We also found that SCF

Indexed as

Amino Acid MotifsBinding SitesCell Cycle ProteinsCell Line, TumorCentriolesCentrosomeF-Box-WD Repeat-Containing Protein 7G1 PhaseGene DuplicationHumansProtein BindingRNA InterferenceRNA, Small InterferingS PhaseSubstrate SpecificityUbiquitinCell Cycle ProteinsF-Box-WD Repeat-Containing Protein 7FBXW7 protein, humanRNA, Small InterferingSASS6 protein, humanUbiquitincell divisioncentriolecentrosomeE3 ubiquitin ligaseF-Box and WD repeat domain-containing 7 (FBXW7)human SAS-6 centriolar assembly protein (HsSAS6)mitosismitotic spindleprocentrioleubiquitin

Identifiers

PMID32086376
PMCPMC7135989
OpenAlexW3006812691

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.