Fascin Conclusion

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Through the creation of Phylogency trees, it was found that fascin 1 was is a protein specific to Eukaryotic organisms. Fascin evolution occured early as it was found within the Animalia kingdom. Even subkingdoms of Animalia were found to have fascin 1 protein and thus it can be determined that Fascin 1 could be first identified with then first Eukaryotic organisms. However due to Fascin 1 not being found with other orders of life, the protein was formed after the Last Common Ancestor.

Structurally little is known about the binding of Fascin to its target molecule actin. An attempt was made to deduce this site through amalgamation of binding pocket analysis, residue conservation, electrostatic surface analysis and through currently known research (of which there is fairly little). The proposed binding sites are localised to residues 136-143 and 386-395 on both subgroups (they are the same molecule back to back). The back to back subgroup model fits well with the action of Fascin as it's actin crossbundling function means it must bind two actin molecules at diametrically opposing ends of itself. (Aratyn Y et.al. 2007). Other important sites include Ser39 which is the PKC phosphorylation site used for activation/deactivation of actin binding function (Ono S et.al. 1997)

Fascin serves a critical role in the formation and opperation of filopodia, spikes, lamellipodial ribs, oocyte microvilli, dendrites and agressive carcinoma movement in the human body (Tseng Y et.al. 2001). Further investigation into the relationships with other proteins involved and to help confirm actin binding regions for the Fascin molecule for its bundling and cross-linking function is definitely warranted because of its prominent role in human bodily processes.

Abstract | Introduction | Methods | Results | Discussion | Conclusion | References
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