Farnesylation of Cenp-F is required for G2/M progression and degradation after mitosis

Deema Hussein, Stephen S. Taylor

    Research output: Contribution to journalArticlepeer-review


    Farnesyl transferase inhibitors induce G2/M cell cycle delays that cannot be explained by inhibition of the Ras GTPase. Recently, the kinetochore protein Cenp-F has been shown to be farnesylated. Here, we show that ectopic expression of the kinetochore targeting domain of Cenp-F delays progression through G2/M. Significantly, this is dependent on the CAAX farnesylation motif. We also show that localisation of Cenp-F to the nuclear envelope at G2/M and kinetochores in prometaphase is dependent both on its CAAX motif and farnesyl transferase activity. Strikingly, farnesyl transferase activity is also required for Cenp-F degradation after mitosis. Thus, these observations suggest that farnesylation of Cenp-F is required not only for its localisation to the nuclear envelope and kinetochores but also for timely progression through G2/M and its degradation after mitosis. In addition, these observations raise the possibility that the anti-proliferative effects induced by farnesyl transferase inhibitors may be due to inhibition of Cenp-F function and/or turnover.
    Original languageEnglish
    Pages (from-to)3403-3414
    Number of pages11
    JournalJournal of Cell Science
    Issue number17
    Publication statusPublished - 1 Sept 2002


    • Cenp-F
    • Farnesyl transferase inhibitor
    • Kinetochore
    • Mitosis
    • Protein farnesylation


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