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

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Iuzzolino, Angela, Pellegrini, Francesca Romana, Rotili, Dante, Degrassi, Francesca, Trisciuoglio, Daniela·2024·Cellular and Molecular Life Sciences
DOI 10.1007/s00018-024-05227-xPMC PMC11039541
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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.

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Cited by

Sorted by citations

Authors
Iuzzolino, A., Pellegrini, F. R., Rotili, D., Degrassi, F., & Trisciuoglio, D.
Affiliations
  • Institute of Molecular Biology and Pathology (IT)
  • Sapienza University of Rome (IT)
Corresponding author
  • Degrassi, Francesca
  • Trisciuoglio, Daniela
ORCID
Venue
Cellular and Molecular Life Sciences
Publisher
Springer Science and Business Media LLC
Published
2024-04-23
Volume
81
Issue
1
Pages
193-193
ISSN
  • 1420-682X (ISSN-L)
  • 1420-9071
DOI
10.1007/s00018-024-05227-x
PMC
PMC11039541
OpenAlex
W4395048974
Cited by
33
References
5
Citations by year
2026: 17 · 2025: 10 · 2024: 6
FWCI
1.74
Type
journal article
Language
en
Open access
Licence
Locations
  • Cellular and Molecular Life Sciences (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • IRIS Research product catalog (Sapienza University of Rome) (submittedVersion, cc-by)
  • Iris (Roma Tre University) (submittedVersion)
Funders
Consiglio Nazionale Delle Ricerche
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
  • Physical Sciences › Chemistry › Organic Chemistry › Synthesis and biological activity
Keywords
alpha-tubulin acetylation, post-translational modification, microtubule stability, enzyme structure, substrate binding, cell motility, mitosis, cytoskeletal organization, intracellular trafficking, human disease
MeSH terms
Acetylation, Acetyltransferases, Animals, Cell Movement, Cytoskeleton, Humans, Microtubule Proteins, Microtubules, Mitosis, Neoplasms, Protein Processing, Post-Translational, Tubulin

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