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

Baker, Karen and Kirkham, Sara and Halova, Lenka and Atkin, Jane and Franz-Wachtel, Mirita and Cobley, David and Krug, Karsten and Maček, Boris and Mulvihill, Daniel P. and Petersen, Janni (2016) TOR complex 2 localises to the cytokinetic actomyosin ring and controls the fidelity of cytokinesis. Journal of Cell Science, 129 (13). ISSN 0021-9533. E-ISSN 1477-9137. (doi:https://doi.org/10.1242/jcs.190124) (Full text available)

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Abstract

The timing of cell division is controlled by the coupled regulation of growth and division. The 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 a myosin II, Myp2, and myosin V, Myo51, 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 cytokinetic machinery. We go on to show that TORC2 dependent phosphorylation of Acp1 (Actin Capping Protein, a known regulator of cytokinesis) controls CAR stability and the modulation of CAPZA/BAcp1/2 heterodimer formation and is essential for survival upon stress. Thus TORC2 localisation to the CAR and TORC2 dependent CAPZAAcp1 phosphorylation contributes to timely control and fidelity of cytokinesis and cell division.

Item Type: Article
Subjects: Q Science
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Dan Mulvihill
Date Deposited: 25 May 2016 15:14 UTC
Last Modified: 08 Sep 2016 08:53 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/55693 (The current URI for this page, for reference purposes)
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