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MBC in Press, published online ahead of print August 9, 2006
Mol. Biol. Cell 10.1091/mbc.E05-10-0994

A more recent version of this article appeared on October 1, 2006
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Submitted on October 28, 2005
Revised on June 29, 2006
Accepted on July 31, 2006

WASP-interacting Protein (WIPa) 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

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.

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






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