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MBC in Press, published online ahead of print June 21, 2006
Mol. Biol. Cell 10.1091/mbc.E06-05-0381

A more recent version of this article appeared on September 1, 2006
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Submitted on May 3, 2006
Revised on June 2, 2006
Accepted on June 8, 2006

Guanylyl Cyclase Protein and cGMP Product Independently Control Front and Back of Chemotaxing Dictyostelium Cells

Douwe M. Veltman and Peter J.M. Van Haastert

Department of Biology, University of Groningen, 9751 NN Haren, The Netherlands

Monitoring Editor: Yu-li Wang

Chemotaxis of amoeboid cells is driven by actin filaments in leading pseudopodia and actin-myosin filaments in the back and at the side of the cell to suppress pseudopodia. In Dictyostelium cGMP plays an important role during chemotaxis, and is produced predominantly by a soluble guanylyl cyclase, sGC. The sGC protein is enriched in extending pseudopodia at the leading edge of the cell during chemotaxis. We show here that the sGC protein and the cGMP product have different functions during chemotaxis, using two mutants that lose either catalytic activity (sGC{Delta}cat) or localization to the leading edge (sGC{Delta}N). Cells expressing sGC{Delta}N exhibit excellent cGMP formation and myosin localization in the back of the cell, but exhibit poor orientation at the leading edge. Cells expressing the catalytically dead sGC{Delta}cat mutant show poor myosin localization at the back, but excellent localization of the sGC protein at the leading edge, where it enhances the probability that a new pseudopod is made in close proximity to previous pseudopodia, resulting in a decrease of the degree of turning. Thus cGMP supresses pseudopod formation in the back f the cell, whereas the sGC protein refines pseudopod formation at the leading edge.

Address correspondence to: Peter J.M. Van Haastert (P.J.M.van.haastert{at}rug.nl)




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