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    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.

    Citation

    Rebecca L Gorry, Kieran Brennan, Paul T M Lavin, Tayler Mazurski, Charline Mary, David Matallanas, Jean-Fran├žois Guichou, Margaret M Mc Gee. Cyclophilin A Isomerisation of Septin 2 Mediates Abscission during Cytokinesis. International journal of molecular sciences. 2023 Jul 04;24(13)

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    PMID: 37446263

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