All these pathways involve Wnt ligands binding to Frizzled receptor complexes, and it is likely that Dishevelled to signal Ginsenoside-F5 downstream through distinct biochemical pathways. Linkage of Dsh to the b-catenin pathway involves regulated changes in Dsh stability, phosphorylation, and protein interactions. The net result of these changes is to reduce degradation of non-membrane-associated b-catenin, leading to its accumulation in the nucleus and modulation of gene transcription through interactions with the Lef/Tcf family of transcription factors. In contrast, the PCP and potentially related Wnt/Ca pathways involve Dsh signaling through b-catenin-independent mechanisms. The PCP and Wnt/Ca pathways have many downstream effectors, such as Ca sensitive enzymes, small GTPases, and JNK, which may vary in different cell types, but commonly regulate cell polarity and movement via changes in Orbifloxacin cytoskeletal dynamics. Dsh is conserved in Bilateria and functions in dorsal patterning, cell polarity, gastrulation movements, and neural tube closure. In X. laevis, localization of Dsh to the presumptive dorsal side of the early embryo and subsequent nuclear localization of b-catenin during cleavage stages results in activation of several target genes, including siamois, Xnr3, and Xbra. Thereafter, Xbra induces expression of Wnt11, and downstream b-catenin-independent signaling through Dsh regulates convergent extension movements in the mesoderm and neural ectoderm involved in gastrulation and neural tube closure. Dsh is a modular protein comprised of multiple conserved domains including the DIX, PDZ and DEP domains that have partially separable signaling functions. The DIX domain is an alpha helical motif located near the N-terminus that mediates homo- and hetero-dimerization between Dvl proteins, Axin proteins, Ccd1/DIXDC1 proteins, plus interaction with at least one protein that lacks a DIX domain, Actin. Evidence from different organisms has suggested that the DIX domain is required for Wnt/b-catenin signaling as opposed to b-catenin-independent forms of signaling. In Drosophila melanogaster, the DIX domain is necessary to increase b-catenin levels in the nucleus, but not to rescue PCP pathway defects. In mammalian cells, the DIX domain is required to increase nuclear b-catenin and to activate Tcf/Lefdependent transcription, but not to activate JNK activity.