SUMOylation of α-tubulin is a novel modification regulating microtubule dynamics.
Amino Acids
/ metabolism
Animals
Cell Line
Cysteine Endopeptidases
/ metabolism
Humans
Mice
Microtubules
/ chemistry
Models, Molecular
Neurites
/ metabolism
Neuronal Outgrowth
/ genetics
Protein Binding
Protein Multimerization
Protein Processing, Post-Translational
Solubility
Structure-Activity Relationship
Sumoylation
Tubulin
/ chemistry
SUMOylation
microtubule assembly
microtubule dynamics
α-tubulin
Journal
Journal of molecular cell biology
ISSN: 1759-4685
Titre abrégé: J Mol Cell Biol
Pays: United States
ID NLM: 101503669
Informations de publication
Date de publication:
07 05 2021
07 05 2021
Historique:
received:
12
11
2020
revised:
02
12
2020
accepted:
14
12
2020
pubmed:
5
1
2021
medline:
18
1
2022
entrez:
4
1
2021
Statut:
ppublish
Résumé
Microtubules (MTs) are regulated by a number of known posttranslational modifications (PTMs) on α/β-tubulin to fulfill diverse cellular functions. Here, we showed that SUMOylation is a novel PTM on α-tubulin in vivo and in vitro. The SUMOylation on α-tubulin mainly occurred at Lys 96 (K96), K166, and K304 of soluble α-tubulin and could be removed by small ubiquitin-related modifier (SUMO)-specific peptidase 1. In vitro experiments showed that tubulin SUMOylation could reduce interprotofilament interaction, promote MT catastrophe, and impede MT polymerization. In cells, mutation of the SUMOylation sites on α-tubulin reduced catastrophe frequency and increased the proportion of polymerized α-tubulin, while upregulation of SUMOylation with fusion of SUMO1 reduced α-tubulin assembly into MTs. Additionally, overexpression of SUMOylation-deficient α-tubulin attenuated the neurite extension in Neuro-2a cells. Thus, SUMOylation on α-tubulin represents a new player in the regulation of MT properties.
Identifiants
pubmed: 33394042
pii: 6062403
doi: 10.1093/jmcb/mjaa076
pmc: PMC8104938
doi:
Substances chimiques
Amino Acids
0
Tubulin
0
SENP1 protein, human
EC 3.4.-
Cysteine Endopeptidases
EC 3.4.22.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
91-103Informations de copyright
© The Author(s) (2021). Published by Oxford University Press on behalf of Journal of Molecular Cell Biology, CEMCS, CAS.
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