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Originally published as MBC in Press, 10.1091/mbc.E05-10-0994 on August 9, 2006

Vol. 17, Issue 10, 4564-4575, October 2006

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WASP-interacting Protein Is Important for Actin Filament Elongation and Prompt Pseudopod Formation in Response to a Dynamic Chemoattractant Gradient

Scott A. Myers, Laura R. Leeper, and Chang Y. Chung

Department of Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232-6600

Submitted October 28, 2005; Revised June 29, 2006; Accepted July 31, 2006
Monitoring Editor: Martin A. Schwartz

The role of WASP-interacting protein (WIP) in the process of F-actin assembly during chemotaxis of Dictyostelium was examined. Mutations of the WH1 domain of WASP led to a reduction in binding to WIPa, a newly identified homolog of mammalian WIP, a reduction of F-actin polymerization at the leading edge, and a reduction in chemotactic efficiency. WIPa localizes to sites of new pseudopod protrusion and colocalizes with WASP at the leading edge. WIPa increases F-actin elongation in vivo and in vitro in a WASP-dependent manner. WIPa translocates to the cortical membrane upon uniform cAMP stimulation in a time course that parallels F-actin polymerization. WIPa-overexpressing cells exhibit multiple microspike formation and defects in chemotactic efficiency due to frequent changes of direction. Reduced expression of WIPa by expressing a hairpin WIPa (hp WIPa) construct resulted in more polarized cells that exhibit a delayed response to a new chemoattractant source due to delayed extension of pseudopod toward the new gradient. These results suggest that WIPa is required for new pseudopod protrusion and prompt reorientation of cells toward a new gradient by initiating localized bursts of actin polymerization and/or elongation.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06-05-0376) on August 9, 2006.

Address correspondence to: Chang Y. Chung (Chang.Chung{at}Vanderbilt.edu)






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