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.
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January 24 2025
Arginylation of ⍺-tubulin at E77 regulates microtubule dynamics via MAP1S
Brittany MacTaggart
,
Brittany MacTaggart
(Conceptualization, Formal analysis, Investigation, Methodology, Validation, Visualization, Writing - original draft, Writing - review & editing)
1
University of Pennsylvania, School of Veterinary Medicine
, Philadelphia, PA, USA
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Junling Wang
,
Junling Wang
(Conceptualization, Resources, Supervision)
1
University of Pennsylvania, School of Veterinary Medicine
, Philadelphia, PA, USA
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Hsin-Yao Tang
,
Hsin-Yao Tang
(Investigation, Resources, Writing - review & editing)
2
Proteomics and Metabolomics Facility, Wistar Institute
, Philadelphia, PA, USA
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Anna Kashina
(Conceptualization, Data curation, Funding acquisition, Methodology, Project administration, Supervision, Visualization, Writing - original draft, Writing - review & editing)
1
University of Pennsylvania, School of Veterinary Medicine
, Philadelphia, PA, USA
Correspondence to Anna Kashina: [email protected]
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Brittany MacTaggart
Conceptualization, Formal analysis, Investigation, Methodology, Validation, Visualization, Writing - original draft, Writing - review & editing
1
University of Pennsylvania, School of Veterinary Medicine
, Philadelphia, PA, USA
Junling Wang
Conceptualization, Resources, Supervision
1
University of Pennsylvania, School of Veterinary Medicine
, Philadelphia, PA, USA
Hsin-Yao Tang
Investigation, Resources, Writing - review & editing
2
Proteomics and Metabolomics Facility, Wistar Institute
, Philadelphia, PA, USA
Correspondence to Anna Kashina: [email protected]
Disclosures: The authors declare no competing interests exist.
Received:
June 18 2024
Revision Received:
November 26 2024
Accepted:
January 03 2025
Online ISSN: 1540-8140
Print ISSN: 0021-9525
Funding
Funder(s):
National Institutes of Health
- Award Id(s): R35GM122505,R01NS102435,T32 GM007229
© 2025 MacTaggart et al.
2025
MacTaggart et al.
This article is distributed under the terms as described at https://rupress.org/pages/terms102024/.
J Cell Biol (2025) 224 (4): e202406099.
Article history
Received:
June 18 2024
Revision Received:
November 26 2024
Accepted:
January 03 2025
Citation
Brittany MacTaggart, Junling Wang, Hsin-Yao Tang, Anna Kashina; Arginylation of ⍺-tubulin at E77 regulates microtubule dynamics via MAP1S. J Cell Biol 3 April 2025; 224 (4): e202406099. doi: https://doi.org/10.1083/jcb.202406099
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