Plo1 kinase recruitment to the spindle pole body and its role in cell division in Schizosaccharomyces pombe

Mulvihill, Daniel P. and Petersen, Janni and Ohkura, Hiroyuki and Glover, David M. and Hagan, Iain M. (1999) Plo1 kinase recruitment to the spindle pole body and its role in cell division in Schizosaccharomyces pombe. Molecular Biology of the Cell, 10 (8). pp. 2771-85. ISSN 1059-1524 . (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1091/mbc.10.8.2771

Abstract

Polo kinases execute multiple roles during cell division. The fission yeast polo related kinase Plo1 is required to assemble the mitotic spindle, the prophase actin ring that predicts the site for cytokinesis and for septation after the completion of mitosis (Ohkura et al., 1995; Bahler et al., 1998). We show that Plo1 associates with the mitotic but not interphase spindle pole body (SPB). SPB association of Plo1 is the earliest fission yeast mitotic event recorded to date. SPB association is strong from mitotic commitment to early anaphase B, after which the Plo1 signal becomes very weak and finally disappears upon spindle breakdown. SPB association of Plo1 requires mitosis-promoting factor (MPF) activity, whereas its disassociation requires the activity of the anaphase-promoting complex. The stf1.1 mutation bypasses the usual requirement for the MPF activator Cdc25 (Hudson et al., 1990). Significantly, Plo1 associates inappropriately with the interphase SPB of stf1.1 cells. These data are consistent with the emerging theme from many systems that polo kinases participate in the regulation of MPF to determine the timing of commitment to mitosis and may indicate that pole association is a key aspect of Plo1 function. Plo1 does not associate with the SPB when septation is inappropriately driven by deregulation of the Spg1 pathway and remains SPB associated if septation occurs in the presence of a spindle. Thus, neither Plo1 recruitment to nor its departure from the SPB are required for septation; however, overexpression of plo1+ activates the Spg1 pathway and causes transient Cdc7 recruitment to the SPB and multiple rounds of septation.

Item Type: Article
Additional information: 1059-1524 (Print) Journal Article Research Support, Non-U.S. Gov't
Uncontrolled keywords: Basic-Leucine Zipper Transcription Factors CDC2 Protein Kinase/metabolism Cell Cycle Proteins/metabolism Cell Division/physiology DNA-Binding Proteins/genetics/metabolism *Drosophila Proteins GTP Phosphohydrolases/metabolism Interphase/physiology Ligases/metabolism Maturation-Promoting Factor/metabolism Mitosis/physiology Mitotic Spindle Apparatus/*metabolism Phosphoprotein Phosphatases/metabolism Protein-Serine-Threonine Kinases/*metabolism Schizosaccharomyces/cytology/*metabolism *Soybean Proteins *Ubiquitin-Protein Ligase Complexes Ubiquitin-Protein Ligases cdc25 Phosphatases
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Dan Mulvihill
Date Deposited: 14 Jun 2009 16:10
Last Modified: 30 Apr 2014 13:46
Resource URI: http://kar.kent.ac.uk/id/eprint/8907 (The current URI for this page, for reference purposes)
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