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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).
References:-
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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