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First identified in Drosophila (Wellington et al, 1999) the Spire protein consists of four WH2 domains followed by a zinc finger (fig1). Actin is bound by the WH2 domains.  Recent evidence suggest that spire is involved in intracellular transport (Kerkhoff et al, 2001).


Kerkhoff, E., Simpson, J. C., Leberfinger, C. B., Otto, I. M., Doerks, T., Bork, P., Rapp, U. R., Raabe, T. & Pepperkok, R. (2001) The Spir actin organizers are involved in vesicle transport processes., Curr. Biol. 11, 1963-1968.

Otto, I. M., Raabe, T., Rennefahrt, U. E., Bork, P., Rapp, U. R. & Kerkhoff, E. (2000) The p150-Spir protein provides a link between c-jun N-terminal kinase function and actin organization., Curr. Biol. 10, 345-348.

Wellington, A., Emmons, S., James, B., Calley, J., Grover, M., Tolias, P. & Manseau, L. (1999) Spire contains actin binding domains and is related to ascidian posterior end mark-5., Development. 126, 5267-5274.

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