Evidence map›Paper›PMID 35963242›Full record

ArticleCurrent biology : CB2022

EML2-S constitutes a new class of proteins that recognizes and regulates the dynamics of tyrosinated microtubules.

Takashi Hotta, Thomas S McAlear, Yang Yue, Takumi Higaki, Sarah E Haynes, Alexey I Nesvizhskii, David Sept, Kristen J Verhey, Susanne Bechstedt, Ryoma Ohi

Open access · greenAbstract read
In one paragraph

Article in Current biology : CB, 2022. 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
2.8field-weighted citation impact, top 9% 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, 26 citations in OpenAlex.

  1. Article
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  4. Peptide-based covalent inhibitor of tubulin detyrosination promotes mesenchymal-to-epithelial transition in lung cancer cells.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  9. Review
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  14. Comprehensive analysis of EML2 as a prognostic biomarker in colon cancer.International journal of clinical and experimental pathology · 2024
    Article
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  16. Article
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  19. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 3 countries.

Takashi HottaDepartment of Cell and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.
Thomas S McAlearDepartment of Anatomy and Cell Biology, McGill University, Montreal, QC, Canada.
Yang YueDepartment of Cell and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.
Takumi HigakiFaculty of Advanced Science and Technology (FAST), Kumamoto University, Kumamoto, Japan; International Research Organization for Advanced Science and Technology (IROAST), Kumamoto University, Kumamoto, Japan.
Sarah E HaynesDepartment of Pathology, University of Michigan, Ann Arbor, MI, USA.
Alexey I NesvizhskiiDepartment of Pathology, University of Michigan, Ann Arbor, MI, USA; Department of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, MI, USA.
David SeptDepartment of Biomedical Engineering, University of Michigan, Ann Arbor, MI, USA.
Kristen J VerheyDepartment of Cell and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.
Susanne BechstedtDepartment of Anatomy and Cell Biology, McGill University, Montreal, QC, Canada.
Ryoma OhiDepartment of Cell and Developmental Biology, University of Michigan, Ann Arbor, MI, USA. Electronic address: oryoma@umich.edu.
University of Michigan–Ann Arbor · USMcGill University · CAKumamoto University · JP

Funding

Kinesin Motors and Microtubule-based TraffickingR35GM131744 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Kristen J. Verhey · 2019 to 2026
$6.3M
COMPUTATIONAL TOOLS FOR MASS SPECTROMETRY-BASED INTERACTOME DATAR01GM094231 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Alexey I Nesvizhskii · 2010 to 2026
$5.4M
Regulation of microtubule dynamics during cell divisionR01GM086610 · NIGMS · VANDERBILT UNIVERSITY · PI OHI, RYOMA · 2010 to 2023
$4.5M
Dynamic Regulation of the Actin Filament Barbed EndR01GM136822 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SEPT, DAVID · 2020 to 2023
$1.2M
CIHR PJT-156193NIGMS NIH HHS R01 GM086610NIGMS NIH HHS R01 GM094231NIGMS NIH HHS R01 GM136822NIGMS NIH HHS R35 GM131744
6 · The paper itself

Abstract

Tubulin post-translational modifications (PTMs) alter microtubule properties by affecting the binding of microtubule-associated proteins (MAPs). Microtubule detyrosination, which occurs by proteolytic removal of the C-terminal tyrosine from ɑ-tubulin, generates the oldest known tubulin PTM, but we lack comprehensive knowledge of MAPs that are regulated by this PTM. We developed a screening pipeline to identify proteins that discriminate between Y- and ΔY-microtubules and found that echinoderm microtubule-associated protein-like 2 (EML2) preferentially interacts with Y-microtubules. This activity depends on a Y-microtubule interaction motif built from WD40 repeats. We show that EML2 tracks the tips of shortening microtubules, a behavior not previously seen among human MAPs in vivo, and influences dynamics to increase microtubule stability. Our screening pipeline is readily adapted to identify proteins that specifically recognize a wide range of microtubule PTMs.

Indexed as

MicrotubulesTubulinHumansMicrotubule-Associated ProteinsProtein Processing, Post-TranslationalTyrosineEML2 protein, humanMicrotubule-Associated ProteinsTubulinTyrosineechinoderm microtubule-associated proteinmicrotubulepost-translational modificationtubulin codetyrosinationWD repeat

Identifiers

PMID35963242
PMCPMC9530018
OpenAlexW4290839922

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.