Cyclophilin A Isomerisation of Septin 2 Mediates Abscission during Cytokinesis.
cancer
cell division
cyclophilin
cytokinesis
prolyl isomerase
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
04 Jul 2023
04 Jul 2023
Historique:
received:
15
05
2023
revised:
21
06
2023
accepted:
24
06
2023
medline:
17
7
2023
pubmed:
14
7
2023
entrez:
14
7
2023
Statut:
epublish
Résumé
The isomerase activity of Cyclophilin A is important for midbody abscission during cell division, however, to date, midbody substrates remain unknown. In this study, we report that the GTP-binding protein Septin 2 interacts with Cyclophilin A. We highlight a dynamic series of Septin 2 phenotypes at the midbody, previously undescribed in human cells. Furthermore, Cyclophilin A depletion or loss of isomerase activity is sufficient to induce phenotypic Septin 2 defects at the midbody. Structural and molecular analysis reveals that Septin 2 proline 259 is important for interaction with Cyclophilin A. Moreover, an isomerisation-deficient EGFP-Septin 2 proline 259 mutant displays defective midbody localisation and undergoes impaired abscission, which is consistent with data from cells with loss of Cyclophilin A expression or activity. Collectively, these data reveal Septin 2 as a novel interacting partner and isomerase substrate of Cyclophilin A at the midbody that is required for abscission during cytokinesis in cancer cells.
Identifiants
pubmed: 37446263
pii: ijms241311084
doi: 10.3390/ijms241311084
pmc: PMC10341793
pii:
doi:
Substances chimiques
Septins
EC 3.6.1.-
Cyclophilin A
EC 5.2.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Science Foundation Ireland
ID : 11/RFP.1/CAN/3202
Pays : Ireland
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