Evidence map›Paper›PMID 39852692›Full record

ArticleThe Journal of cell biology2025

Arginylation of ⍺-tubulin at E77 regulates microtubule dynamics via MAP1S.

Brittany MacTaggart, Junling Wang, Hsin-Yao Tang, Anna Kashina

Abstract read
In one paragraph

Article in The Journal of cell biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. Method Overview for Discovering ATE1 Substrates and their Arginylation Sites.Chembiochem : a European journal of chemical biology · 2025
    Review
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

4 authors.

Brittany MacTaggartUniversity of Pennsylvania, School of Veterinary Medicine , Philadelphia, PA, USA.ORCID 0000-0001-7674-6042
Junling WangUniversity of Pennsylvania, School of Veterinary Medicine , Philadelphia, PA, USA.ORCID 0000-0002-3391-7144
Hsin-Yao TangProteomics and Metabolomics Facility, Wistar Institute , Philadelphia, PA, USA.ORCID 0000-0003-1838-018X
Anna KashinaUniversity of Pennsylvania, School of Veterinary Medicine , Philadelphia, PA, USA.ORCID 0000-0002-0243-6866

Funding

Tumor Microenvironment and MetastasisP30CA010815 · NCI · WISTAR INSTITUTE · PI Luis J Montaner · 1985 to 2026
$75.9M
TRAINING PROGRAM IN CELL AND MOLECULAR BIOLOGYT32GM007229 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI BARTOLOMEI, MARISA S. · 1985 to 2023
$14.0M
Regulation of cell migration by nucleotide coding sequence and arginylationR35GM122505 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Anna S Kashina · 2017 to 2026
$6.2M
Role of arginylation in prevention of alpha synuclein-driven neurodegenerationR01NS102435 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI KASHINA, ANNA S · 2019 to 2023
$2.6M
Advancing Cancer Research through Comprehensive Proteomics and Metabolomics AnalysesR50CA221838 · NCI · WISTAR INSTITUTE · PI Hsin-Yao Tang · 2017 to 2026
$2.1M
NCI NIH HHS P30 CA010815NCI NIH HHS R50 CA221838NIGMS NIH HHS R35 GM122505NIGMS NIH HHS T32 GM007229NIH HHS R35GM122505NINDS NIH HHS R01 NS102435
6 · The paper itself

Abstract

Arginylation is the posttranslational addition of arginine to a protein by arginyltransferase-1 (ATE1). Previous studies have found that ATE1 targets multiple cytoskeletal proteins, and Ate1 deletion causes cytoskeletal defects, including reduced cell motility and adhesion. Some of these defects have been linked to actin arginylation, but the role of other arginylated cytoskeletal proteins has not been studied. Here, we characterize tubulin arginylation and its role in the microtubule cytoskeleton. We identify ATE1-dependent arginylation of ⍺-tubulin at E77. Ate1-/- cells and cells overexpressing non-arginylatable ⍺-tubulinE77A both show a reduced microtubule growth rate and increased microtubule stability. Additionally, they show an increase in the fraction of the stabilizing protein MAP1S associated with microtubules, suggesting that E77 arginylation directly regulates MAP1S binding. Knockdown of Map1s is sufficient to rescue microtubule growth rate and stability to wild-type levels. Together, these results demonstrate a new type of tubulin regulation by posttranslational arginylation, which modulates microtubule growth rate and stability through the microtubule-associated protein, MAP1S.

Indexed as

ArginineMicrotubule-Associated ProteinsMicrotubulesTubulinAminoacyltransferasesAnimalsHumansMiceProtein Processing, Post-TranslationalAminoacyltransferasesArgininearginyltransferaseMicrotubule-Associated ProteinsTubulin

Identifiers

PMID39852692
PMCPMC11775831

What OpenQuestion holds

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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.