@article {cite-key, title = {A mutational analysis of
dishevelled in Drosophila defines novel domains in the
dishevelled protein as well as novel suppressing alleles of
axin.}, journal = {Genetics}, volume = {161}, number = {2}, year
= {2002}, month = {Jun}, pages = {747{\textendash}762}, address
= {Howard Hughes Medical Institute, Department of Developmental
Biology, Stanford University Medical School, Stanford,
California 94305-5323, USA.}, abstract = {Drosophila dishevelled
(dsh) functions in two pathways: it is necessary to transduce
Wingless (Wg) signaling and it is required in planar cell
polarity. To learn more about how Dsh can discriminate between
these functions, we performed genetic screens to isolate
additional dsh alleles and we examined the potential role of
protein phosphorylation by site-directed mutagenesis. We
identified two alleles with point mutations in the Dsh DEP
domain that specifically disrupt planar polarity signaling. When
positioned in the structure of the DEP domain, these mutatio