Cyclophilin A Isomerisation of Septin 2 Mediates Abscission during Cytokinesis

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...

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Published inInternational journal of molecular sciences Vol. 24; no. 13; p. 11084
Main Authors Gorry, Rebecca L, Brennan, Kieran, Lavin, Paul T M, Mazurski, Tayler, Mary, Charline, Matallanas, David, Guichou, Jean-François, Mc Gee, Margaret M
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 04.07.2023
MDPI
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Summary: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.
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content type line 23
ISSN:1422-0067
1661-6596
1422-0067
1661-6596
DOI:10.3390/ijms241311084