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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Glycogen synthase kinase 3 and h-prune regulate cell migration by modulating focal adhesions.

h-prune, which has been suggested to be involved in cell migration, was identified as a glycogen synthase kinase 3 (GSK-3)-binding protein. Treatment of cultured cells with GSK-3 inhibitors or small interfering RNA (siRNA) for GSK-3 and h-prune inhibited their motility. The kinase activity of GSK-3 was required for the interaction of GSK-3 with h-prune. h-prune was localized to focal adhesions, and the siRNA for GSK-3 or h-prune delayed the disassembly of paxillin. The tyrosine phosphorylation of focal adhesion kinase (FAK) and the activation of Rac were suppressed in GSK-3 or h-prune knocked-down cells. GSK-3 inhibitors suppressed the disassembly of paxillin and the activation of FAK and Rac. Furthermore, h-prune was highly expressed in colorectal and pancreatic cancers, and the positivity of the h-prune expression was correlated with tumor invasion. These results suggest that GSK-3 and h-prune cooperatively regulate the disassembly of focal adhesions to promote cell migration and that h-prune is useful as a marker for tumor aggressiveness.[1]


  1. Glycogen synthase kinase 3 and h-prune regulate cell migration by modulating focal adhesions. Kobayashi, T., Hino, S., Oue, N., Asahara, T., Zollo, M., Yasui, W., Kikuchi, A. Mol. Cell. Biol. (2006) [Pubmed]
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