Dishevelled

Dishevelled specific domain
Solution structure of the mouse Dvl-1 DEP domain based on the PDB: 1fsh​ coordinates.
Identifiers
SymbolDishevelled
PfamPF02377
InterProIPR003351
PROSITEPDOC50841
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1fsh​, 1mc7​, 1l6o​, 2f0a​

Dishevelled (Dsh) is a family of proteins involved in canonical and non-canonical Wnt signalling pathways. Dsh (Dvl in mammals) is a cytoplasmic phosphoprotein that acts directly downstream of frizzled receptors.[1] It takes its name from its initial discovery in flies, where a mutation in the dishevelled gene was observed to cause improper orientation of body and wing hairs.[2] There are vertebrate homologs in zebrafish, Xenopus (Xdsh), mice (Dvl1, -2, -3) and humans (DVL-1, -2, -3). Dsh relays complex Wnt signals in tissues and cells, in normal and abnormal contexts.[2] [3] It is thought to interact with the SPATS1 protein when regulating the Wnt Signalling pathway.[4]

Dishevelled plays important roles in both the embryo and the adult, ranging from cellular differentiation and cell polarity to social behavior.[2]

  1. ^ Penton A, Wodarz A, Nusse R (June 2002). "A mutational analysis of dishevelled in Drosophila defines novel domains in the dishevelled protein as well as novel suppressing alleles of axin". Genetics. 161 (2): 747–62. doi:10.1093/genetics/161.2.747. PMC 1462152. PMID 12072470.
  2. ^ a b c Wallingford JB, Habas R (October 2005). "The developmental biology of Dishevelled: an enigmatic protein governing cell fate and cell polarity". Development. 132 (20): 4421–36. doi:10.1242/dev.02068. PMID 16192308.
  3. ^ Sharma M, Castro-Piedras I, Simmons GE, Pruitt K (July 2018). "Dishevelled: A masterful conductor of complex Wnt signals". Cellular Signalling. 47: 52–64. doi:10.1016/j.cellsig.2018.03.004. PMC 6317740. PMID 29559363.
  4. ^ Zhang H, Zhang H, Zhang Y, Ng SS, Ren F, Wang Y, Duan Y, Chen L, Zhai Y, Guo Q, Chang Z (November 2010). "Dishevelled-DEP domain interacting protein (DDIP) inhibits Wnt signaling by promoting TCF4 degradation and disrupting the TCF4/beta-catenin complex". Cellular Signalling. 22 (11): 1753–60. doi:10.1016/j.cellsig.2010.06.016. PMID 20603214.