Evidence map›Paper›PMID 33826363›Full record

ArticleMolecular biology of the cell2021

Protein turnover dynamics suggest a diffusion-to-capture mechanism for peri-basal body recruitment and retention of intraflagellar transport proteins.

Jaime V K Hibbard, Neftali Vazquez, Rohit Satija, John B Wallingford

Open access · bronzeAbstract read
In one paragraph

Article in Molecular biology of the cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Taking Down the Primary Cilium: Pathways for Disassembly in Differentiating Cells.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. The intraflagellar transport cycle.Nature reviews. Molecular cell biology · 2025
    Review
  7. Article
  8. Permanent cilia loss during cerebellar granule cell neurogenesis involves withdrawal of cilia maintenance and centriole capping.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Article
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  14. Review
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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

4 authors at 2 institutions in 1 country.

Jaime V K HibbardDepartment of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712.
Neftali VazquezDepartment of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712.
Rohit SatijaCalifornia Institute of Quantitative Biosciences, University of California, Berkeley, Berkeley, CA 94720.
John B WallingfordDepartment of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712.
The University of Texas at Austin · USQB3 · US

Funding

Mapping the CPLANE interactome, an extensive protein interaction network underlying human ciliopathiesR01HD085901 · NICHD · UNIVERSITY OF TEXAS AT AUSTIN · PI EDWARD M MARCOTTE, John B Wallingford · 2016 to 2026
$6.2M
Development and function in mucociliary epitheliaR01HL117164 · NHLBI · UNIVERSITY OF TEXAS AT AUSTIN · PI John B Wallingford · 2013 to 2026
$4.7M
NHLBI NIH HHS R01 HL117164NICHD NIH HHS R01 HD085901
6 · The paper itself

Abstract

Intraflagellar transport (IFT) is essential for construction and maintenance of cilia. IFT proteins concentrate at the basal body where they are thought to assemble into trains and bind cargoes for transport. To study the mechanisms of IFT recruitment to this peri-basal body pool, we quantified protein dynamics of eight IFT proteins, as well as five other basal body localizing proteins using fluorescence recovery after photobleaching in vertebrate multiciliated cells. We found that members of the IFT-A and IFT-B protein complexes show distinct turnover kinetics from other basal body components. Additionally, known IFT subcomplexes displayed shared dynamics, suggesting shared basal body recruitment and/or retention mechanisms. Finally, we evaluated the mechanisms of basal body recruitment by depolymerizing cytosolic MTs, which suggested that IFT proteins are recruited to basal bodies through a diffusion-to-capture mechanism. Our survey of IFT protein dynamics provides new insights into IFT recruitment to basal bodies, a crucial step in ciliogenesis and ciliary signaling.

Indexed as

AnimalsBasal BodiesCarrier ProteinsCiliaEmbryo, NonmammalianKineticsProtein TransportSignal TransductionXenopusCarrier Proteins

Identifiers

PMID33826363
PMCPMC8351562
OpenAlexW3143379434

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.