Evidence map›Paper›PMID 25103237›Full record

ArticleMolecular biology of the cell2014

The cytosolic carboxypeptidases CCP2 and CCP3 catalyze posttranslational removal of acidic amino acids.

Olivia Tort, Sebastián Tanco, Cecilia Rocha, Ivan Bièche, Cecilia Seixas, Christophe Bosc, Annie Andrieux, Marie-Jo Moutin, Francesc Xavier Avilés, Julia Lorenzo and 1 more

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

50 citing papers in PubMed, 80 citations in OpenAlex.

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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

11 authors at 5 institutions in 4 countries.

Olivia TortInstitut de Biotecnologia i de Biomedicina, Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, 08193 Bellaterra (Barcelona), Spain Institut Curie, 91405 Orsay, France.
Sebastián TancoInstitut de Biotecnologia i de Biomedicina, Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, 08193 Bellaterra (Barcelona), Spain Department of Medical Protein Research, VIB, 9000 Ghent, Belgium Department of Biochemistry, Ghent University, 9000 Ghent, Belgium.
Cecilia RochaInstitut Curie, 91405 Orsay, France PSL Research University, 75005 Paris, France Centre National de la Recherche Scientifique, UMR3306, 91405 Orsay, France Institut National de la Santé et de la Recherche Médicale, U1005, 91405 Orsay, France.
Ivan BièchePSL Research University, 75005 Paris, France Department of Genetics, Institut Curie, 75248 Paris, France.
Cecilia SeixasCentro de Estudos de Doenças Crónicas, Faculdade de Ciências Médicas, Universidade Nova de Lisboa, 1169-056 Lisbon, Portugal.
Christophe BoscInstitut des Neurosciences de Grenoble, Institut National de la Santé et de la Recherche Médicale, U836, CEA, Université Joseph Fourier, 38042 Grenoble, France Université Grenoble Alpes, 38000 Grenoble, France CEA, Institut de Recherches en Technologies et Sciences pour le Vivant, 38000 Grenoble, France.
Annie AndrieuxInstitut des Neurosciences de Grenoble, Institut National de la Santé et de la Recherche Médicale, U836, CEA, Université Joseph Fourier, 38042 Grenoble, France Université Grenoble Alpes, 38000 Grenoble, France CEA, Institut de Recherches en Technologies et Sciences pour le Vivant, 38000 Grenoble, France.
Marie-Jo MoutinInstitut des Neurosciences de Grenoble, Institut National de la Santé et de la Recherche Médicale, U836, CEA, Université Joseph Fourier, 38042 Grenoble, France Université Grenoble Alpes, 38000 Grenoble, France CEA, Institut de Recherches en Technologies et Sciences pour le Vivant, 38000 Grenoble, France.
Francesc Xavier AvilésInstitut de Biotecnologia i de Biomedicina, Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, 08193 Bellaterra (Barcelona), Spain.
Julia LorenzoInstitut de Biotecnologia i de Biomedicina, Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, 08193 Bellaterra (Barcelona), Spain Julia.Lorenzo@uab.cat Carsten.Janke@curie.fr.
Carsten JankeInstitut Curie, 91405 Orsay, France PSL Research University, 75005 Paris, France Centre National de la Recherche Scientifique, UMR3306, 91405 Orsay, France Institut National de la Santé et de la Recherche Médicale, U1005, 91405 Orsay, France Julia.Lorenzo@uab.cat Carsten.Janke@curie.fr.
Universitat Autònoma de Barcelona · ESInserm · FRCentre National de la Recherche Scientifique · FRUniversidade Nova de Lisboa · PTUniversité Paris Sciences et Lettres · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The posttranslational modification of carboxy-terminal tails of tubulin plays an important role in the regulation of the microtubule cytoskeleton. Enzymes responsible for deglutamylating tubulin have been discovered within a novel family of mammalian cytosolic carboxypeptidases. The discovery of these enzymes also revealed the existence of a range of other substrates that are enzymatically deglutamylated. Only four of six mammalian cytosolic carboxypeptidases had been enzymatically characterized. Here we complete the functional characterization of this protein family by demonstrating that CCP2 and CCP3 are deglutamylases, with CCP3 being able to hydrolyze aspartic acids with similar efficiency. Deaspartylation is a novel posttranslational modification that could, in conjunction with deglutamylation, broaden the range of potential substrates that undergo carboxy-terminal processing. In addition, we show that CCP2 and CCP3 are highly regulated proteins confined to ciliated tissues. The characterization of two novel enzymes for carboxy-terminal protein modification provides novel insights into the broadness of this barely studied process.

Indexed as

Actin CytoskeletonAmino Acid SequenceAnimalsAspartic AcidCarboxypeptidasesCatalytic DomainCell LineCiliaGlutamic AcidGranzymesHEK293 CellsHumansMiceMice, KnockoutMicrotubulesProtein Processing, Post-TranslationalAspartic AcidCarboxypeptidasesGlutamic AcidGranzymesGzmc protein, mouseGzme protein, mouse

Identifiers

PMID25103237
PMCPMC4230590
OpenAlexW2111441789

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.