Báo cáo sinh học: "Nuclear localization is required for Dishevelled function in Wnt/ -catenin signaling"

Tuyển tập các báo cáo nghiên cứu về sinh học được đăng trên tạp chí sinh học Journal of Biology đề tài: Nuclear localization is required for Dishevelled function in Wnt/ -catenin signaling. | J. Biol. Journal of Biology BioMed Central Research article Open Access Nuclear localization is required for Dishevelled function in Wnt 0-catenin signaling Keiji Itoh Barbara K Brott Gyu-Un Bae Marianne J Ratcliffe and Sergei Y Sokol f Addresses Department of Microbiology and Molecular Genetics Harvard Medical School and Beth Israel Deaconess Medical Center Boston MA 02215 USA. Current address Department of Molecular Cell and Developmental Biology Mount Sinai School of Medicine Box 1020 One Gustave L. Levy Place New York NY 10029 USA. Correspondence Sergei Y Sokol. E-mail Received 29 June 2004 Revised 30 November 2004 Accepted 22 December 2004 Published 15 February 2005 Journal of Biology 2005 4 3 The electronic version of this article is the complete one and can be found online at http content 4 1 3 2005 Itoh et al. licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background Dishevelled Dsh is a key component of multiple signaling pathways that are initiated by Wnt secreted ligands and Frizzled receptors during embryonic development. Although Dsh has been detected in a number of cellular compartments the importance of its subcellular distribution for signaling remains to be determined. Results We report that Dsh protein accumulates in cell nuclei when Xenopus embryonic explants or mammalian cells are incubated with inhibitors of nuclear export or when a specific nuclear-export signal NES in Dsh is disrupted by mutagenesis. Dsh protein with a mutated NES while predominantly nuclear remains fully active in its ability to stimulate canonical Wnt signaling. Conversely point mutations in conserved amino-acid residues that are essential for the nuclear localization of Dsh impair the .

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