Evidence map›Paper›PMID 38652325›Full record

ReviewCellular and molecular life sciences : CMLS2024

The α-tubulin acetyltransferase ATAT1: structure, cellular functions, and its emerging role in human diseases.

Angela Iuzzolino, Francesca Romana Pellegrini, Dante Rotili, Francesca Degrassi, Daniela Trisciuoglio

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2024. 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
–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

19 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Microtubule inner proteins in apicomplexan parasites.Biochemical Society transactions · 2026
    Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Tubulin Acetylation: A Critical Regulator of Microtubule Function.Results and problems in cell differentiation · 2025
    Review
  16. Review
  17. Article
  18. Article
  19. Article
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

5 authors.

Angela Iuzzolino *IBPM Institute of Molecular Biology and Pathology, CNR National Research Council of Italy, Via degli Apuli 4, Rome, 00185, Italy.ORCID http://orcid.org/0000-0002-3470-3180
Francesca Romana Pellegrini *IBPM Institute of Molecular Biology and Pathology, CNR National Research Council of Italy, Via degli Apuli 4, Rome, 00185, Italy.ORCID http://orcid.org/0000-0003-4030-5127
Dante RotiliDepartment of Drug Chemistry & Technologies, Sapienza University of Rome, Piazzale Aldo Moro 5, Rome, 00185, Italy.ORCID http://orcid.org/0000-0002-8428-8763
Francesca DegrassiIBPM Institute of Molecular Biology and Pathology, CNR National Research Council of Italy, Via degli Apuli 4, Rome, 00185, Italy. francesca.degrassi@cnr.it.ORCID http://orcid.org/0000-0002-9312-0794
Daniela TrisciuoglioIBPM Institute of Molecular Biology and Pathology, CNR National Research Council of Italy, Via degli Apuli 4, Rome, 00185, Italy. daniela.trisciuoglio@cnr.it.ORCID http://orcid.org/0000-0002-7007-7914

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The acetylation of α-tubulin on lysine 40 is a well-studied post-translational modification which has been associated with the presence of long-lived stable microtubules that are more resistant to mechanical breakdown. The discovery of α-tubulin acetyltransferase 1 (ATAT1), the enzyme responsible for lysine 40 acetylation on α-tubulin in a wide range of species, including protists, nematodes, and mammals, dates to about a decade ago. However, the role of ATAT1 in different cellular activities and molecular pathways has been only recently disclosed. This review comprehensively summarizes the most recent knowledge on ATAT1 structure and substrate binding and analyses the involvement of ATAT1 in a variety of cellular processes such as cell motility, mitosis, cytoskeletal organization, and intracellular trafficking. Finally, the review highlights ATAT1 emerging roles in human diseases and discusses ATAT1 potential enzymatic and non-enzymatic roles and the current efforts in developing ATAT1 inhibitors.

Indexed as

AcetyltransferasesMicrotubule ProteinsTubulinAcetylationAnimalsCell MovementCytoskeletonHumansMicrotubulesMitosisNeoplasmsProtein Processing, Post-TranslationalAcetyltransferasesalpha-tubulin acetylaseATAT1 protein, humanMicrotubule ProteinsTubulinAcetyltransferaseCancerCytoskeletonMicrotubulesNeurological diseasesTubulin acetylation

Identifiers

PMID38652325
PMCPMC11039541

What OpenQuestion holds

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LicenceCC BY
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.