Evidence map›Paper›PMID 25018876›Full record

ArticleCilia2014

Identification of conserved, centrosome-targeting ASH domains in TRAPPII complex subunits and TRAPPC8.

Kenneth B Schou, Stine K Morthorst, Søren T Christensen, Lotte B Pedersen

Open access · hybridAbstract read
In one paragraph

Article in Cilia, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

29 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
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  9. Review
  10. NovelFrontiers in endocrinology · 2023
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  12. A combinedCell cycle (Georgetown, Tex.) · 2022
    Article
  13. Metabolic Dysregulation and Sperm Motility in Male Infertility.Advances in experimental medicine and biology · 2022
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. The unity and diversity of the ciliary central apparatus.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020
    Article
  20. 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

4 authors at 1 institution in 1 country.

Kenneth B SchouDepartment of Biology, University of Copenhagen, Universitetsparken 13, Copenhagen, Denmark ; Center for Experimental Bioinformatics, Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark.
Stine K MorthorstDepartment of Biology, University of Copenhagen, Universitetsparken 13, Copenhagen, Denmark.
Søren T ChristensenDepartment of Biology, University of Copenhagen, Universitetsparken 13, Copenhagen, Denmark.
Lotte B PedersenDepartment of Biology, University of Copenhagen, Universitetsparken 13, Copenhagen, Denmark.
University of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAssembly of primary cilia relies on vesicular trafficking towards the cilium base and intraflagellar transport (IFT) between the base and distal tip of the cilium. Recent studies have identified several key regulators of these processes, including Rab GTPases such as Rab8 and Rab11, the Rab8 guanine nucleotide exchange factor Rabin8, and the transport protein particle (TRAPP) components TRAPPC3, -C9, and -C10, which physically interact with each other and function together with Bardet Biedl syndrome (BBS) proteins in ciliary membrane biogenesis. However, despite recent advances, the exact molecular mechanisms by which these proteins interact and target to the basal body to promote ciliogenesis are not fully understood.

resultsWe surveyed the human proteome for novel ASPM, SPD-2, Hydin (ASH) domain-containing proteins. We identified the TRAPP complex subunits TRAPPC8, -9, -10, -11, and -13 as novel ASH domain-containing proteins. In addition to a C-terminal ASH domain region, we predict that the N-terminus of TRAPPC8, -9, -10, and -11, as well as their yeast counterparts, consists of an α-solenoid bearing stretches of multiple tetratricopeptide (TPR) repeats. Immunofluorescence microscopy analysis of cultured mammalian cells revealed that exogenously expressed ASH domains, as well as endogenous TRAPPC8, localize to the centrosome/basal body. Further, depletion of TRAPPC8 impaired ciliogenesis and GFP-Rabin8 centrosome targeting.

conclusionsOur results suggest that ASH domains confer targeting to the centrosome and cilia, and that TRAPPC8 has cilia-related functions. Further, we propose that the yeast TRAPPII complex and its mammalian counterpart are evolutionarily related to the bacterial periplasmic trafficking chaperone PapD of the usher pili assembly machinery.

Indexed as

ASH domainCentrosomeCiliaGolgiMSP domainRab8Rabin8TPR repeatTRAPPII complexVesicle trafficking

Identifiers

PMID25018876
PMCPMC4094338
OpenAlexW2090462805

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.