Evidence map›Paper›PMID 37386282›Full record

ArticleNature chemistry2023

Tubulin engineering by semi-synthesis reveals that polyglutamylation directs detyrosination.

Eduard Ebberink, Simon Fernandes, Georgios Hatzopoulos, Ninad Agashe, Po-Han Chang, Nora Guidotti, Timothy M Reichart, Luc Reymond, Marie-Claire Velluz, Fabian Schneider and 5 more

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Nature chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.8field-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

19 citing papers in PubMed, 31 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

15 authors at 3 institutions in 2 countries.

Eduard Ebberink *École Polytechnique Fédérale de Lausanne (EPFL), SB ISIC LCBM, Lausanne, Switzerland.
Simon Fernandes *Department of Biochemistry, University of Geneva, Geneva, Switzerland.ORCID 0009-0003-3846-1304
Georgios HatzopoulosSwiss Institute for Experimental Cancer Research (ISREC), EPFL, Lausanne, Switzerland.ORCID 0000-0003-4382-4459
Ninad AgasheÉcole Polytechnique Fédérale de Lausanne (EPFL), SB ISIC LCBM, Lausanne, Switzerland.
Po-Han ChangÉcole Polytechnique Fédérale de Lausanne (EPFL), SB ISIC LCBM, Lausanne, Switzerland.
Nora GuidottiÉcole Polytechnique Fédérale de Lausanne (EPFL), SB ISIC LCBM, Lausanne, Switzerland.
Timothy M ReichartÉcole Polytechnique Fédérale de Lausanne (EPFL), SB ISIC LCBM, Lausanne, Switzerland.ORCID 0000-0002-4015-1925
Luc ReymondBiomolecular Screening Facility, EPFL, Lausanne, Switzerland.ORCID 0000-0001-5282-9273
Marie-Claire VelluzDepartment of Biochemistry, University of Geneva, Geneva, Switzerland.
Fabian SchneiderSwiss Institute for Experimental Cancer Research (ISREC), EPFL, Lausanne, Switzerland.ORCID 0000-0002-3146-4815
Cédric PourroyÉcole Polytechnique Fédérale de Lausanne (EPFL), SB ISIC LCBM, Lausanne, Switzerland.ORCID 0009-0009-1101-126X
Carsten JankeInstitut Curie, Université PSL, CNRS UMR3348, Orsay, France.
Pierre GönczySwiss Institute for Experimental Cancer Research (ISREC), EPFL, Lausanne, Switzerland.
Beat FierzÉcole Polytechnique Fédérale de Lausanne (EPFL), SB ISIC LCBM, Lausanne, Switzerland. beat.fierz@epfl.ch.ORCID 0000-0002-2991-3044
Charlotte AumeierDepartment of Biochemistry, University of Geneva, Geneva, Switzerland. charlotte.aumeier@unige.ch.ORCID 0000-0002-0629-1721
École Polytechnique Fédérale de Lausanne · CHUniversity of Geneva · CHCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microtubules, a critical component of the cytoskeleton, carry post-translational modifications (PTMs) that are important for the regulation of key cellular processes. Long-lived microtubules, in neurons particularly, exhibit both detyrosination of α-tubulin and polyglutamylation. Dysregulation of these PTMs can result in developmental defects and neurodegeneration. Owing to a lack of tools to study the regulation and function of these PTMs, the mechanisms that govern such PTM patterns are not well understood. Here we produce fully functional tubulin carrying precisely defined PTMs within its C-terminal tail. We ligate synthetic α-tubulin tails-which are site-specifically glutamylated-to recombinant human tubulin heterodimers by applying a sortase- and intein-mediated tandem transamidation strategy. Using microtubules reconstituted with these designer tubulins, we find that α-tubulin polyglutamylation promotes its detyrosination by enhancing the activity of the tubulin tyrosine carboxypeptidase vasohibin/small vasohibin-binding protein in a manner dependent on the length of polyglutamyl chains. We also find that modulating polyglutamylation levels in cells results in corresponding changes in detyrosination, corroborating the link between the detyrosination cycle to polyglutamylation.

Indexed as

MicrotubulesTubulinHumansProtein BindingProtein Processing, Post-TranslationalTubulin

Identifiers

PMID37386282
OpenAlexW4382541682

What OpenQuestion holds

Textmetadata
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.