Evidence map›Paper›PMID 27306797›Full record

ArticleNature communications2016

Molecular basis for CPAP-tubulin interaction in controlling centriolar and ciliary length.

Xiangdong Zheng, Anand Ramani, Komal Soni, Marco Gottardo, Shuangping Zheng, Li Ming Gooi, Wenjing Li, Shan Feng, Aruljothi Mariappan, Arpit Wason and 11 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
5.1field-weighted citation impact, top 5% 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

43 citing papers in PubMed, 81 citations in OpenAlex.

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  16. Review
  17. Appearing and disappearing acts of cilia.Journal of biosciences · 2023
    Review
  18. Article
  19. Article
  20. Structural convergence for tubulin binding of CPAP and vinca domain microtubule inhibitors.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

21 authors at 7 institutions in 3 countries.

Xiangdong ZhengBeijing Advanced Innovation Center for Structural Biology, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing 100084, China.
Anand RamaniInstitute for Biochemistry I and Center for Molecular Medicine of the University of Cologne, Robert-Koch-Str. 21, Cologne 50931, Germany.
Komal SoniInstitute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstr. 1, Neuherberg 85764, Germany.
Marco GottardoDepartment of Life Sciences, University of Siena, Siena 53100, Italy.
Shuangping ZhengBeijing Advanced Innovation Center for Structural Biology, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing 100084, China.
Li Ming GooiInstitute for Biochemistry I and Center for Molecular Medicine of the University of Cologne, Robert-Koch-Str. 21, Cologne 50931, Germany.
Wenjing LiMOE Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Shan FengMOE Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Aruljothi MariappanInstitute for Biochemistry I and Center for Molecular Medicine of the University of Cologne, Robert-Koch-Str. 21, Cologne 50931, Germany.
Arpit WasonInstitute for Biochemistry I and Center for Molecular Medicine of the University of Cologne, Robert-Koch-Str. 21, Cologne 50931, Germany.
Per WidlundMax Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauer Str. 108, Dresden 01307, Germany.
Andrei PozniakovskyMax Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauer Str. 108, Dresden 01307, Germany.
Ina PoserMax Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauer Str. 108, Dresden 01307, Germany.
Haiteng DengMOE Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Guangshuo OuMOE Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Maria RiparbelliDepartment of Life Sciences, University of Siena, Siena 53100, Italy.
Callaini GiulianoDepartment of Life Sciences, University of Siena, Siena 53100, Italy.
Anthony A HymanMax Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauer Str. 108, Dresden 01307, Germany.
Michael SattlerInstitute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstr. 1, Neuherberg 85764, Germany.ORCID 0000-0002-1594-0527
Jay GopalakrishnanInstitute for Biochemistry I and Center for Molecular Medicine of the University of Cologne, Robert-Koch-Str. 21, Cologne 50931, Germany.
Haitao LiBeijing Advanced Innovation Center for Structural Biology, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing 100084, China.ORCID 0000-0002-6686-1677
University of Cologne · DECenter for Life Sciences · CNMax Planck Institute of Molecular Cell Biology and Genetics · DEUniversity of Siena · ITCenter for Integrated Protein Science Munich · DETsinghua University · CNSichuan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Centrioles and cilia are microtubule-based structures, whose precise formation requires controlled cytoplasmic tubulin incorporation. How cytoplasmic tubulin is recognized for centriolar/ciliary-microtubule construction remains poorly understood. Centrosomal-P4.1-associated-protein (CPAP) binds tubulin via its PN2-3 domain. Here, we show that a C-terminal loop-helix in PN2-3 targets β-tubulin at the microtubule outer surface, while an N-terminal helical motif caps microtubule's α-β surface of β-tubulin. Through this, PN2-3 forms a high-affinity complex with GTP-tubulin, crucial for defining numbers and lengths of centriolar/ciliary-microtubules. Surprisingly, two distinct mutations in PN2-3 exhibit opposite effects on centriolar/ciliary-microtubule lengths. CPAP(F375A), with strongly reduced tubulin interaction, causes shorter centrioles and cilia exhibiting doublet- instead of triplet-microtubules. CPAP(EE343RR) that unmasks the β-tubulin polymerization surface displays slightly reduced tubulin-binding affinity inducing over-elongation of newly forming centriolar/ciliary-microtubules by enhanced dynamic release of its bound tubulin. Thus CPAP regulates delivery of its bound-tubulin to define the size of microtubule-based cellular structures using a 'clutch-like' mechanism.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCattleCentriolesCiliaCloning, MolecularCrystallography, X-RayEscherichia coliGene ExpressionHeLa CellsHumansMicrotubule-Associated ProteinsMicrotubulesModels, MolecularMutationCENPJ protein, humanMicrotubule-Associated ProteinsProtein IsoformsRecombinant ProteinsTubulin

Identifiers

PMID27306797
PMCPMC4912634
OpenAlexW2422201302

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Registered trials

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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.