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Parsons, M. et al.

Parsons, Monypenny, Ameer-Beg, Millard, Machesky, Peter, Keppler, Schiavo, Watson, Chernoff, Zicha, Vojnovic, Ng,

Spatially distinct binding of Cdc42 to PAK1 and N-WASP in breast carcinoma cells.

While a significant amount is known about the biochemical signaling pathways of the Rho family GTPase Cdc42, a better understanding of how these signaling networks are coordinated in cells is required. In particular, the predominant subcellular sites where GTP-bound Cdc42 binds to its effectors, such as p21-activated kinase 1 ( PAK1) and N-WASP, a homolog of the Wiskott-Aldritch syndrome protein, are still undetermined. Recent fluorescence resonance energy transfer (FRET) imaging experiments using activity biosensors show inconsistencies between the site of local activity of PAK1 or N-WASP and the formation of specific membrane protrusion structures in the cell periphery. The data presented here demonstrate the localization of interactions by using multiphoton time-domain fluorescence lifetime imaging microscopy (FLIM). Our data here establish that activated Cdc42 interacts with PAK1 in a nucleotide-dependent manner in the cell periphery, leading to Thr-423 phosphorylation of PAK1, particularly along the lengths of cell protrusion structures. In contrast, the majority of GFP-N-WASP undergoing FRET with Cy3-Cdc42 is localized within a transferrin receptor- and Rab11-positive endosomal compartment in breast carcinoma cells. These data reveal for the first time distinct spatial association patterns between Cdc42 and its key effector proteins controlling cytoskeletal remodeling.[1]

References

Spatially distinct binding of Cdc42 to PAK1 and N-WASP in breast carcinoma cells. Parsons, M., Monypenny, J., Ameer-Beg, S.M., Millard, T.H., Machesky, L.M., Peter, M., Keppler, M.D., Schiavo, G., Watson, R., Chernoff, J., Zicha, D., Vojnovic, B., Ng, T. Mol. Cell. Biol. (2005) [Pubmed]

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