InterPro : IPR008339

Name  Dishevelled family Short Name  Dishevelled_fam
Type  Family Description  Wnt proteins constitute a large family of secreted signalling molecules thatare involved in intercellular signalling during development. The name derives from the first 2 members of the family to be discovered: int-1 (mouse) and wingless (Wg) (Drosophila) []. It is now recognised that Wnt signalling controls many cell fate decisions in a variety of different organisms, including mammals. Wnt signalling has been implicated in tumourigenesis, early mesodermal patterning of the embryo, morphogenesis of the brain and kidneys, regulation of mammary gland proliferation and Alzheimer's disease [].Wnt signal transduction proceeds initially via binding to their cellsurface receptors - the so-called frizzled proteins. This activates thesignalling functions of B-catenin and regulates the expression of specificgenes important in development []. More recently, however, several non-canonical Wnt signalling pathways have been elucidated that act independently of B-catenin. In both cases, the transduction mechanismrequires dishevelled protein (Dsh), a cytoplasmic phosphoprotein that actsdirectly downstream of frizzled []. In addition to its role in Wnt signalling, Dshis also involved in generating planar polarity in Drosophila and has been implicated in the Notch signal transduction cascade. Three human and mouse homologues of Dsh have been cloned (DVL-1 to 3); it is believed that these proteins, like their Drosophila counterpart, are involved in signal transduction. Human and murine orthologues share more than 95% sequence identity and are each 40-50% identical to Drosophila Dsh.Sequence similarity amongst Dsh proteins is concentrated around three conserved domains: at the N terminus lies a DIX domain (mutations mapping to this region reduce or completely disrupt Wg signalling); a PDZ (or DHR) domain, often found in proteins involved in protein-protein interactions, lies within the central portion of the protein (point mutations within this module have been shown to have little effect on Wg-mediated signal transduction); and a DEP domain is located towards the C terminus and is conserved among a set of proteins that regulate various GTPases (whilst genetic and molecular assays have shown this module to be dispensable for Wg signalling, it is thought to be important in planar polarity signalling in flies []). Therefore the requirement of these domains for distinct signaling pathways varies: the DIX domain is essential for B-catenin activation, the DEP domain is implicated in the activation of the JNK pathway, while the PDZ domain is requiredfor both [].
 Feedback

Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

4 Child Features

Id Name Short Name Type
IPR026542 Dishevelled Dsh Dsh Family
IPR008341 Dishevelled-2 DVL2 Family
IPR008340 Dishevelled-1 DVL-1 Family
IPR008342 Dishevelled-3 DVL3 Family

5 Contains

Id Name Short Name Type
IPR011991 Winged helix-turn-helix DNA-binding domain WHTH_DNA-bd_dom Domain
IPR001158 DIX domain DIX Domain
IPR001478 PDZ domain PDZ Domain
IPR000591 DEP domain DEP_dom Domain
IPR003351 Dishevelled protein domain Dishevelled_protein_dom Domain

0 Found In

1 Parent Features

Id Name Short Name Type
IPR015506 Dishevelled-related protein Dsh/Dvl-rel Family

5 Publications

First Author Title Year Journal Volume Pages
Wodarz A Mechanisms of Wnt signaling in development. 1998 Annu Rev Cell Dev Biol 14 59-88
De Ferrari GV Wnt signaling function in Alzheimer's disease. 2000 Brain Res Brain Res Rev 33 1-12
Peifer M Wnt signaling in oncogenesis and embryogenesis--a look outside the nucleus. 2000 Science 287 1606-9
Penton A A mutational analysis of dishevelled in Drosophila defines novel domains in the dishevelled protein as well as novel suppressing alleles of axin. 2002 Genetics 161 747-62
Li L Dishevelled proteins lead to two signaling pathways. Regulation of LEF-1 and c-Jun N-terminal kinase in mammalian cells. 1999 J Biol Chem 274 129-34



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)