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A critical role for the type V myosin, Myo52, in septum deposition and cell fission during cytokinesis in Schizosaccharomyces pombe.

Mulvihill, Daniel P., Edwards, Suzanne R., Hyams, Jeremy S. (2006) A critical role for the type V myosin, Myo52, in septum deposition and cell fission during cytokinesis in Schizosaccharomyces pombe. Cell Motility and the Cytoskeleton, 63 . pp. 149-161. ISSN 0886-1544. E-ISSN 1097-0169. (doi:10.1002/cm.20113) (Access to this publication is currently restricted. You may be able to access a copy if URLs are provided)

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Cytokinesis in fission yeast involves the coordination of septum deposition with the contraction of a cytokinetic actomyosin ring. We have examined the role of the type V myosin Myo52 in the coupling of these two events by the construction of a series of deletion mutants of the Myo52 tail and a further mutant within the ATP binding domain of the head. Each mutant protein was ectopically expressed in fission yeast cells. Each truncation was assayed for the ability to localize to the cell poles and septum (the normal cellular locations of Myo52) and to rescue the morphology defects and temperature sensitivity of a myo52Delta strain. A region within the Myo52 tail (amino acids 1320-1503), with a high degree of similarity to the vesicle-binding domain of the budding yeast type V myosin Myo2p, was essential for Myo52's role in the maintenance of growth polarity and cell division. A separate region (amino acids 1180-1320) was required for Myo52 foci to move throughout the cytoplasm; however, constructs lacking this region, but which retained the ability to dimerize still associated with actin at sites of cell growth. Not all of the Myo52 truncations which localized rescued the morphological defects of myo52Delta, demonstrating that loss of function was not simply brought about by an inability of mutant proteins to target the correct cellular location. By contrast, Myo52 motor activity was required for both localization and cellular function. myo52Delta cells were unable to efficiently localize the beta-1,3-glucan synthase, Bgs1, either at the cell poles or at the division septum, regions of cell wall deposition. Bgs1 and Myo52 localized to vesicle-like dots at the poles in interphase and these moved together to the septum at division. These data have led to the formulation of a model in which Myo52 is responsible for the delivery of Bgs1 and associated molecules to polar cell growth regions during interphase. On the commencement of septum formation, Myo52 transports Bgs1 to the cell equator, thus ensuring the accurate deposition of beta-1,3-glucan at the leading edge of the primary septum.

Item Type: Article
DOI/Identification number: 10.1002/cm.20113
Subjects: Q Science
Divisions: Faculties > Sciences > School of Biosciences > Cell & Developmental Biology Group
Depositing User: Sue Davies
Date Deposited: 19 Dec 2007 17:50 UTC
Last Modified: 28 May 2019 13:34 UTC
Resource URI: (The current URI for this page, for reference purposes)
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