Researchers have identified that Dishevelled doesn’t only function in the cytoplasm and at the cell membrane – it must also pass into the nucleus. A study published today in Journal of Biology reveals that Dishevelled, a key player in the Wnt/beta-catenin signalling pathway, has to be localised in the nucleus to perform a key aspect of its function. This discovery should shed light on both normal embryonic development and the development of cancer.
In the paper, Sergei Sokol and colleagues, from Harvard Medical School, show that Dishevelled (Dsh) is constantly shuttling between the nucleus and the cytoplasm, owing to its nuclear export and import sequences, but that it has to be in the nucleus to respond to certain Wnt signals transmitted through the ‘canonical’ Wnt signalling pathway.
Dsh has always been considered to be a cytoplasmic protein, exerting its function as a stabiliser of beta-catenin in the cell cytoplasm after stimulation by Wnt secreted ligands binding to Frizzled receptors on the cell surface.
Juliette Savin | alfa
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