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First published online 17 January 2006
doi: 10.1242/jcs.02755

Journal of Cell Science 119, 425-432 (2006)
Published by The Company of Biologists 2006
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Research Article

ARAP3 is essential for formation of lamellipodia after growth factor stimulation

Sonja Krugmann*, Simon Andrews, Len Stephens and Phillip T. Hawkins

The Inositide Laboratory, The Babraham Institute, Cambridge, CB2 4AT, UK

* Author for correspondence (e-mail: sonja.krugmann{at}bbsrc.ac.uk)

Accepted 24 October 2005

Rho and Arf family small GTPases control dynamic actin rearrangements and vesicular trafficking events. ARAP3 is a dual GAP for RhoA and Arf6 that is regulated by phosphatidylinositol (3,4,5)-trisphosphate [PtdIns(3,4,5)P3], a product of the phosphoinositide 3-kinase (PI3K) signalling pathway. To investigate the physiological function of ARAP3, we used an RNAi-based approach in an endothelial cell model. ARAP3-deficient cells showed increased activities of RhoA and Arf6. Phenotypically, they were more rounded than control counterparts and displayed very fine stress fibres. ARAP3-deficient cells were not capable of producing lamellipodia upon growth factor stimulation, a process known to depend on PI3K and Rac activities. Rac was transiently activated in stimulated ARAP3 RNAi cells although its cellular localisation was altered, a likely consequence of increased Arf6 activity. We conclude that ARAP3 recruitment to sites of elevated PtdIns(3,4,5)P3 is crucial to allow localised inactivation of RhoA and cycling of Arf6, both of which are necessary to allow growth factor-stimulated formation of lamellipodia.

Key words: GTPase-activating protein, ARAP3, PI3K, Rho, Arf, Lamellipodium




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