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Vol. 8, Issue 12, 2617-2629, December 1997
Department of Biochemistry, Stanford University, Stanford,
California 94305
We have investigated the role of myosin in cytokinesis in
Dictyostelium cells by examining cells under both
adhesive and nonadhesive conditions. On an adhesive surface, both
wild-type and myosin-null cells undergo the normal processes of mitotic
rounding, cell elongation, polar ruffling, furrow ingression, and
separation of daughter cells. When cells are denied adhesion through
culturing in suspension or on a hydrophobic surface, wild-type cells
undergo these same processes. However, cells lacking myosin round up
and polar ruffle, but fail to elongate, furrow, or divide. These
differences show that cell division can be driven by two mechanisms
that we term Cytokinesis A, which requires myosin, and Cytokinesis B,
which is cell adhesion dependent. We have used these approaches to
examine cells expressing a myosin whose two light chain-binding sites were deleted (
BLCBS-myosin). Although this myosin is a slower motor
than wild-type myosin and has constitutively high activity due to the
abolition of regulation by light-chain phosphorylation, cells
expressing BLCBS-myosin were previously shown to divide in
suspension (). However, we suspected
their behavior during cytokinesis to be different from wild-type cells given the large alteration in their myosin. Surprisingly,
BLCBS-myosin undergoes relatively normal spatial and temporal
changes in localization during mitosis. Furthermore, the rate of furrow
progression in cells expressing a BLCBS-myosin is similar to that in
wild-type cells.
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