DEP domains: structurally similar but functionally different

Nat Rev Mol Cell Biol. 2014 May;15(5):357-62. doi: 10.1038/nrm3791. Epub 2014 Apr 16.

Abstract

The Dishevelled, EGL-10 and pleckstrin (DEP) domain is a globular protein domain that is present in about ten human protein families with well-defined structural features. A picture is emerging that DEP domains mainly function in the spatial and temporal control of diverse signal transduction events by recruiting proteins to the plasma membrane. DEP domains can interact with various partners at the membrane, including phospholipids and membrane receptors, and their binding is subject to regulation.

Publication types

  • Review

MeSH terms

  • Adaptor Proteins, Signal Transducing / chemistry
  • Adaptor Proteins, Signal Transducing / genetics
  • Adaptor Proteins, Signal Transducing / metabolism*
  • Animals
  • Caenorhabditis elegans / genetics
  • Caenorhabditis elegans / metabolism
  • Cell Membrane / metabolism
  • Dishevelled Proteins
  • Drosophila Proteins
  • Drosophila melanogaster / genetics
  • Drosophila melanogaster / metabolism
  • Gene Expression Regulation
  • Guanine Nucleotide Exchange Factors / chemistry
  • Guanine Nucleotide Exchange Factors / genetics
  • Guanine Nucleotide Exchange Factors / metabolism*
  • Humans
  • Models, Molecular
  • Phosphoproteins / chemistry
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Protein Binding
  • Protein Structure, Tertiary
  • RGS Proteins / chemistry
  • RGS Proteins / genetics
  • RGS Proteins / metabolism*
  • Signal Transduction*

Substances

  • Adaptor Proteins, Signal Transducing
  • Dishevelled Proteins
  • Drosophila Proteins
  • Guanine Nucleotide Exchange Factors
  • PREX1 protein, human
  • Phosphoproteins
  • RAPGEF3 protein, human
  • RGS Proteins
  • dsh protein, Drosophila