Evidence map›Paper›PMID 26412126›Full record

ArticleCurrent biology : CB2015

A Short CEP135 Splice Isoform Controls Centriole Duplication.

Kristin D Dahl, Divya Ganapathi Sankaran, Brian A Bayless, Mary E Pinter, Domenico F Galati, Lydia R Heasley, Thomas H Giddings, Chad G Pearson

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
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  9. Human centrosome organization and function in interphase and mitosis.Seminars in cell & developmental biology · 2021
    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

8 authors at 2 institutions in 1 country.

Kristin D DahlDepartment of Cell and Developmental Biology, University of Colorado School of Medicine, 2801 East 17(th) Avenue, Aurora, CO 80045-2537, USA.
Divya Ganapathi SankaranDepartment of Cell and Developmental Biology, University of Colorado School of Medicine, 2801 East 17(th) Avenue, Aurora, CO 80045-2537, USA.
Brian A BaylessDepartment of Cell and Developmental Biology, University of Colorado School of Medicine, 2801 East 17(th) Avenue, Aurora, CO 80045-2537, USA.
Mary E PinterDepartment of Cell and Developmental Biology, University of Colorado School of Medicine, 2801 East 17(th) Avenue, Aurora, CO 80045-2537, USA.
Domenico F GalatiDepartment of Cell and Developmental Biology, University of Colorado School of Medicine, 2801 East 17(th) Avenue, Aurora, CO 80045-2537, USA.
Lydia R HeasleyDepartment of Cell and Developmental Biology, University of Colorado School of Medicine, 2801 East 17(th) Avenue, Aurora, CO 80045-2537, USA.
Thomas H GiddingsMCD Biology, University of Colorado at Boulder, 347 UCB, Boulder, CO 80309-0347, USA.
Chad G PearsonDepartment of Cell and Developmental Biology, University of Colorado School of Medicine, 2801 East 17(th) Avenue, Aurora, CO 80045-2537, USA. Electronic address: chad.pearson@ucdenver.edu.
University of Colorado Denver · USUniversity of Colorado Boulder · US

Funding

Mechanisms of centriole assembly and stabilityR01GM099820 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI PEARSON, CHAD G · 2012 to 2020
$2.9M
NIGMS NIH HHS GM099820NIGMS NIH HHS R01 GM099820
6 · The paper itself

Abstract

Centriole duplication is coordinated such that a single round of duplication occurs during each cell cycle. Disruption of this synchrony causes defects including supernumerary centrosomes in cancer and perturbed ciliary signaling [1-5]. To preserve the normal number of centrioles, the level, localization, and post-translational modification of centriole proteins is regulated so that, when centriole protein expression and/or activity are increased, centrioles self-assemble. Assembly is initiated by the formation of the cartwheel structure that comprises the base of centrioles [6-11]. SAS-6 constitutes the cartwheel, and SAS-6 levels remain low until centriole assembly is initiated at S phase onset [3, 12, 13]. CEP135 physically links to SAS-6 near the site of microtubule nucleation and binds to CPAP for triplet microtubule formation [13, 14]. We identify two distinct protein isoforms of CEP135 that antagonize each other to modulate centriole duplication: full-length CEP135 (CEP135(full)) promotes new assembly, whereas a short isoform, CEP135(mini), represses it. CEP135(mini) represses centriole duplication by limiting the centriolar localization of CEP135(full) binding proteins (SAS-6 and CPAP) and the pericentriolar localization of γ-tubulin. The CEP135 isoforms exhibit distinct and complementary centrosomal localization during the cell cycle. CEP135(mini) protein decreases from centrosomes upon anaphase onset. We suggest that the decrease in CEP135(mini) from centrosomes promotes centriole assembly. The repression of centriole duplication by a splice isoform of a protein that normally promotes it serves as a novel mechanism to limit centriole duplication.

Indexed as

Carrier ProteinsCell CycleCell Cycle ProteinsCentriolesCentrosomeHeLa CellsHumansMicrotubule-Associated ProteinsMicrotubulesProtein BindingProtein IsoformsRNA SplicingS PhaseTubulinCarrier ProteinsCell Cycle ProteinsCEP135 protein, humanMicrotubule-Associated ProteinsProtein IsoformsSASS6 protein, humanTubulin

Identifiers

PMID26412126
PMCPMC4596786
OpenAlexW2103330295

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.