Evidence map›Paper›PMID 36636822›Full record

ArticleThe EMBO journal2023

Tubulin polyglutamylation differentially regulates microtubule-interacting proteins.

Mariya Genova, Lenka Grycova, Verena Puttrich, Maria M Magiera, Zdenek Lansky, Carsten Janke, Marcus Braun

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
9.1field-weighted citation impact, top 2% 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

40 citing papers in PubMed, 61 citations in OpenAlex.

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  12. An Orthogonal Way of Writing the Tubulin Code.Cytoskeleton (Hoboken, N.J.) · 2026
    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

7 authors at 2 institutions in 2 countries.

Mariya Genova *Institut Curie, Université PSL, CNRS UMR3348, Orsay, France.ORCID 0000-0003-4209-4239
Lenka Grycova *Institute of Biotechnology, Czech Academy of Sciences, BIOCEV, Prague West, Czech Republic.ORCID 0000-0002-6476-3627
Verena PuttrichInstitute of Biotechnology, Czech Academy of Sciences, BIOCEV, Prague West, Czech Republic.
Maria M MagieraInstitut Curie, Université PSL, CNRS UMR3348, Orsay, France.ORCID 0000-0003-4847-3053
Zdenek LanskyInstitute of Biotechnology, Czech Academy of Sciences, BIOCEV, Prague West, Czech Republic.
Carsten JankeInstitut Curie, Université PSL, CNRS UMR3348, Orsay, France.ORCID 0000-0001-7053-2000
Marcus BraunInstitute of Biotechnology, Czech Academy of Sciences, BIOCEV, Prague West, Czech Republic.ORCID 0000-0003-2026-2238
Czech Academy of Sciences, Institute of Biotechnology · CZCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tubulin posttranslational modifications have been predicted to control cytoskeletal functions by coordinating the molecular interactions between microtubules and their associating proteins. A prominent tubulin modification in neurons is polyglutamylation, the deregulation of which causes neurodegeneration. Yet, the underlying molecular mechanisms have remained elusive. Here, using in-vitro reconstitution, we determine how polyglutamylation generated by the two predominant neuronal polyglutamylases, TTLL1 and TTLL7, specifically modulates the activities of three major microtubule interactors: the microtubule-associated protein Tau, the microtubule-severing enzyme katanin and the molecular motor kinesin-1. We demonstrate that the unique modification patterns generated by TTLL1 and TTLL7 differentially impact those three effector proteins, thus allowing for their selective regulation. Given that our experiments were performed with brain tubulin from mouse models in which physiological levels and patterns of polyglutamylation were altered by the genetic knockout of the main modifying enzymes, our quantitative measurements provide direct mechanistic insight into how polyglutamylation could selectively control microtubule interactions in neurons.

Indexed as

TubulinAnimalsCytoskeletonKinesinsMiceMicrotubule-Associated ProteinsMicrotubulesPeptide SynthasesKinesinsMicrotubule-Associated ProteinsPeptide SynthasesTubulintubulin polyglutamylasekataninkinesin-1microtubule-associated Taumicrotubulespolyglutamylationtubulin posttranslational modifications

Identifiers

PMID36636822
PMCPMC9975938
OpenAlexW4315927691

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.