Introduction

The long-term goal of our research is to determine how myosin motors function in cytokinesis, a complex event that ensures the physical separation of dividing cells at the end of the cell cycle. Our lab is focused on the function and regulation of conventional myosin (myosin-II), the motor that together with actin filaments forms the contractile ring. This highly dynamic actomyosin structure, along with many associated factors powers constriction at the cell division site.

Live cell imaging of fission yeast cells by fluorescence microscopy. The actomyosin contractile ring assembles as a broad band of nodes, which coalesce to form a tight ring that constricts to pinch the cell in two. The contractile ring is marked by green fluorescent protein (GFP) fused to the UCS protein (Rng3p), a Myo2p regulator.

Myosin-II plays an essential role in a large variety of fundamental cellular processes, often exhibiting more specialized roles depending on cell-type. We employ both budding and fission yeast as our model systems. Fission yeast is an especially attractive model since it not only offers the advantages of robust and well-established molecular genetics and cell biology, but it also provides a unique and convenient setting in which the only known role for myosin-II lies in cytokinesis. Information obtained on fission yeast myosin-II function will provide answers at the molecular level as to how the myosin-II motor is designed for cytokinesis.

Investigations in the laboratory utilize a wide range of techniques including molecular biology, yeast genetics, cell biology, biochemistry and biophysics.

University of Vermont
Health Science Research Facility
Dept. of Molecular Physiology & Biophysics
Burlington, Vermont 05405
phone 802-656-9898; fax 802-656-0747

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