Evidence map›Paper›PMID 23644468›Full record

ArticleNature cell biology2013

CEP162 is an axoneme-recognition protein promoting ciliary transition zone assembly at the cilia base.

Won-Jing Wang, Hwee Goon Tay, Rajesh Soni, Geoffrey S Perumal, Mary G Goll, Frank P Macaluso, John M Asara, Jeffrey D Amack, Meng-Fu Bryan Tsou

Open access · greenAbstract read
In one paragraph

Article in Nature cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

64 citing papers in PubMed, 101 citations in OpenAlex.

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  4. The kinesin-4 protein KIF27 forms a cytoskeletal scaffold at the transition zone to promote motile cilia structural integrity.Proceedings of the National Academy of Sciences of the United States of America · 2025
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4 more citing papers are in PubMed but not listed here.

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

9 authors at 4 institutions in 1 country.

Won-Jing WangCell Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA.
Hwee Goon Tay
Rajesh Soni
Geoffrey S Perumal
Mary G Goll
Frank P Macaluso
John M Asara
Jeffrey D Amack
Meng-Fu Bryan Tsou
Memorial Sloan Kettering Cancer Center · USAlbert Einstein College of Medicine · USSUNY Upstate Medical University · USHarvard University · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
The Control of Centriole Duplication and DegenerationR01GM088253 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI MENG-FU BRYAN TSOU · 2009 to 2026
$6.2M
Regulation of Ciliated Cells that Control Cardiac LateralityR01HL095690 · NHLBI · UPSTATE MEDICAL UNIVERSITY · PI AMACK, JEFFREY D · 2009 to 2014
$1.7M
NCI NIH HHS P30 CA008748NHLBI NIH HHS HL095690NHLBI NIH HHS R01 HL095690NIGMS NIH HHS GM088253NIGMS NIH HHS R01 GM088253
6 · The paper itself

Abstract

The transition zone is a specialized compartment found at the base of cilia, adjacent to the centriole distal end, where axonemal microtubules are heavily crosslinked to the surrounding membrane to form a barrier that gates the ciliary compartment. A number of ciliopathy molecules have been found to associate with the transition zone, but factors that directly recognize axonemal microtubules to specify transition zone assembly at the cilia base remain unclear. Here, through quantitative centrosome proteomics, we identify an axoneme-associated protein, CEP162 (KIAA1009), tethered specifically at centriole distal ends to promote transition zone assembly. CEP162 interacts with core transition zone components, and mediates their association with microtubules. Loss of CEP162 arrests ciliogenesis at the stage of transition zone assembly. Abolishing its centriolar tethering, however, allows CEP162 to stay on the growing end of the axoneme and ectopically assemble transition zone components at cilia tips. This generates extra-long cilia with strikingly swollen tips that actively release ciliary contents into the extracellular environment. CEP162 is thus an axoneme-recognition protein pre-tethered at centriole distal ends before ciliogenesis to promote and restrict transition zone formation specifically at the cilia base.

Indexed as

3T3 CellsAdenosine TriphosphatasesAnimalsAntigens, NeoplasmAxonemeCell Cycle ProteinsCell LineCentriolesCentrosomeCiliaCytoskeletal ProteinsHeLa CellsHumansMembrane ProteinsMiceMicrotubule-Associated ProteinsAdenosine TriphosphatasesAntigens, NeoplasmCell Cycle ProteinsCEP162 protein, humanCep290 protein, humanCytoskeletal ProteinsMembrane ProteinsMicrotubule-Associated ProteinsMicrotubule ProteinsNeoplasm ProteinsRNA, Small Interfering

Identifiers

PMID23644468
PMCPMC3815462
OpenAlexW2086857229

What OpenQuestion holds

Textmetadata
LicenceTDM
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.