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Originally published as MBC in Press, 10.1091/mbc.E07-07-0663 on January 9, 2008

Vol. 19, Issue 3, 1125-1138, March 2008

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The Actomyosin Ring Recruits Early Secretory Compartments to the Division Site in Fission Yeast

Aleksandar Vjestica*,{dagger}, Xin-Zi Tang*, and Snezhana Oliferenko*

*Cell Dynamics Group, Temasek Life Sciences Laboratory, 117604 Singapore and {dagger}Department of Biological Sciences, National University of Singapore, 117543 Singapore

Submitted July 13, 2007; Revised December 17, 2007; Accepted December 27, 2007
Monitoring Editor: Daniel Lew

The ultimate goal of cytokinesis is to establish a membrane barrier between daughter cells. The fission yeast Schizosaccharomyces pombe utilizes an actomyosin-based division ring that is thought to provide physical force for the plasma membrane invagination. Ring constriction occurs concomitantly with the assembly of a division septum that is eventually cleaved. Membrane trafficking events such as targeting of secretory vesicles to the division site require a functional actomyosin ring suggesting that it serves as a spatial landmark. However, the extent of polarization of the secretion apparatus to the division site is presently unknown. We performed a survey of dynamics of several fluorophore-tagged proteins that served as markers for various compartments of the secretory pathway. These included markers for the endoplasmic reticulum, the COPII sites, and the early and late Golgi. The secretion machinery exhibited a marked polarization to the division site. Specifically, we observed an enrichment of the transitional endoplasmic reticulum (tER) accompanied by Golgi cisternae biogenesis. These processes required actomyosin ring assembly and the function of the EFC-domain protein Cdc15p. Cdc15p overexpression was sufficient to induce tER polarization in interphase. Thus, fission yeast polarizes its entire secretory machinery to the cell division site by utilizing molecular cues provided by the actomyosin ring.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E07-07-0663) on January 9, 2008.

Address correspondence to: Snezhana Oliferenko (snejana{at}tll.org.sg)




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