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Published online November 26, 2007
doi:10.1083/jcb.200705068
The Journal of Cell Biology, Vol. 179, No. 5, 833-843
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Jeon et al.
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 Regulation of Rap1 activity by RapGAP1 controls cell adhesion at the front of chemotaxing cells

Taeck J. Jeon1, Dai-Jen Lee1, Susan Lee1, 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, Canada V6T 1Z3

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

Spatial and temporal regulation of Rap1 is required for proper myosin assembly and cell adhesion during cell migration in Dictyostelium discoideum. Here, we identify a Rap1 guanosine triphosphatase–activating protein (GAP; RapGAP1) that helps mediate cell adhesion by negatively regulating Rap1 at the leading edge. Defects in spatial regulation of the cell attachment at the leading edge in rapGAP1– (null) cells or cells overexpressing RapGAP1 (RapGAP1OE) lead to defective chemotaxis. rapGAP1– cells have extended chemoattractant-mediated Rap1 activation kinetics and decreased MyoII assembly, whereas RapGAP1OE cells show reciprocal phenotypes. We see that RapGAP1 translocates to the cell cortex in response to chemoattractant stimulation and localizes to the leading edge of chemotaxing cells via an F-actin–dependent pathway. RapGAP1 localization is negatively regulated by Ctx, an F-actin bundling protein that functions during cytokinesis. Loss of Ctx leads to constitutive and uniform RapGAP1 cortical localization. We suggest that RapGAP1 functions in the spatial and temporal regulation of attachment sites through MyoII assembly via regulation of Rap1–guanosine triphosphate.

Abbreviations used in this paper: GAP, GTPase–activating protein; GDS, guanine nucleotide dissociation inhibitor; PI3K, phosphoinositide-3 kinase; RBD, Rap binding domain.


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