TOR complex 2 localises to the cytokinetic actomyosin ring and controls the fidelity of cytokinesis

K Barker, S Kirkham, L Halova, J Atkin, M Franz-Wachtel, D Cobley, Karsten Krug, B Macek, DM Mulvihill, Janni Petersen

    Research output: Contribution to journalArticlepeer-review

    15 Citations (Scopus)


    The timing of cell division is controlled by the coupled regulation of growth and division. The target of rapamycin (TOR) signalling network synchronises these processes with the environmental setting. Here, we describe a novel interaction of the fission yeast TOR complex 2 (TORC2) with the cytokinetic actomyosin ring (CAR), and a novel role for TORC2 in regulating the timing and fidelity of cytokinesis. Disruption of TORC2 or its localisation results in defects in CAR morphology and constriction. We provide evidence that the myosin II protein Myp2 and themyosin V proteinMyo51 play roles in recruiting TORC2 to the CAR. We show that Myp2 and TORC2 are co-dependent upon each other for their normal localisation to the cytokineticmachinery.We go on to show that TORC2-dependent phosphorylation of actin-capping protein 1 (Acp1, a known regulator of cytokinesis) controls CAR stability, modulates Acp1-Acp2 (the equivalent of the mammalian CAPZA- CAPZB) heterodimer formation and is essential for survival upon stress. Thus, TORC2 localisation to the CAR, and TORC2-dependent Acp1 phosphorylation contributes to timely control and the fidelity of cytokinesis and cell division.

    Original languageEnglish
    Pages (from-to)2613-2624
    Number of pages12
    JournalJournal of Cell Science
    Issue number13
    Publication statusPublished - 2016


    • Acp1
    • CAPZA
    • Myosin II
    • Myosin V
    • Rictor
    • Schizosaccharomyces pombe
    • TOR
    • TORC2


    Dive into the research topics of 'TOR complex 2 localises to the cytokinetic actomyosin ring and controls the fidelity of cytokinesis'. Together they form a unique fingerprint.

    Cite this