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Published online
doi:10.1083/jcb.200607072
The Journal of Cell Biology, Vol. 176, No. 7, 1021-1033
The Rockefeller University Press, 0021-9525 $30.00
© Jeon et al.
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Article

Rap1 controls cell adhesion and cell motility through the regulation of myosin II



Taeck J. Jeon1, Dai-Jen Lee1, Sylvain Merlot1, Gerald Weeks2, and Richard A. Firtel1

1 Section of Cell and Developmental Biology, Division of Biological Sciences, Center for Molecular Genetics, University of California, San Diego, La Jolla, CA 92093
2 Department of Microbiology and Immunology, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada

Correspondence to Richard A. Firtel: rafirtel{at}ucsd.edu

We have investigated the role of Rap1 in controlling chemotaxis and cell adhesion in Dictyostelium discoideum. Rap1 is activated rapidly in response to chemoattractant stimulation, and activated Rap1 is preferentially found at the leading edge of chemotaxing cells. Cells expressing constitutively active Rap1 are highly adhesive and exhibit strong chemotaxis defects, which are partially caused by an inability to spatially and temporally regulate myosin assembly and disassembly. We demonstrate that the kinase Phg2, a putative Rap1 effector, colocalizes with Rap1–guanosine triphosphate at the leading edge and is required in an in vitro assay for myosin II phosphorylation, which disassembles myosin II and facilitates filamentous actin–mediated leading edge protrusion. We suggest that Rap1/Phg2 plays a role in controlling leading edge myosin II disassembly while passively allowing myosin II assembly along the lateral sides and posterior of the cell.

S. Merlot's present address is Institut des Sciences du Végétal, Centre National de la Recherche Scientifique, 91190 Gif-sur-Yvette, France.

Abbreviations used in this paper: cGMP, cyclic guanosine monophosphate; F-actin, filamentous actin; GEF, guanine nucleotide exchange factor; MHCK, myosin II heavy chain kinase; PH, pleckstrin homology; RA, Ras association; RBD, Ras-binding domain.


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