For whom the bell tolls? DING proteins in health and disease

Cell Mol Life Sci. 2009 Jul;66(14):2205-18. doi: 10.1007/s00018-009-0006-6. Epub 2009 Mar 17.

Abstract

DING proteins, identified mainly by their eponymous N-terminal sequences, are ubiquitous in living organisms. Amongst bacteria, they are common in pseudomonads, and have been characterised with respect to genetics and structure. They form part of a wider family of phosphate-binding proteins, with emerging roles in phosphate acquisition and pathogenicity. Many DING proteins have been isolated in eukaryotes, in which they have been associated with very diverse biological activities, often in the context of possible signalling roles. Disease states in which DING proteins have been implicated include rheumatoid arthritis, lithiasis, atherosclerosis, some tumours and tumour-associated cachexia, and bacterial and viral adherence. Complete genetic and structural characterisation of eukaryotic DING genes and proteins is still lacking, though the phosphate-binding site seems to be conserved. Whether as bacterial proteins related to bacterial pathogenicity, or as eukaryotic components of biochemical signalling systems, DING proteins require further study.

Publication types

  • Review

MeSH terms

  • Animals
  • DNA-Binding Proteins* / chemistry
  • DNA-Binding Proteins* / genetics
  • DNA-Binding Proteins* / metabolism
  • Disease*
  • Escherichia coli Proteins* / chemistry
  • Escherichia coli Proteins* / genetics
  • Escherichia coli Proteins* / metabolism
  • Forecasting
  • Health*
  • Humans
  • Models, Molecular
  • Polycomb Repressive Complex 1
  • Protein Binding / genetics
  • Protein Structure, Tertiary / genetics
  • Repressor Proteins* / chemistry
  • Repressor Proteins* / genetics
  • Repressor Proteins* / metabolism
  • Structure-Activity Relationship
  • Ubiquitin-Protein Ligases* / chemistry
  • Ubiquitin-Protein Ligases* / genetics
  • Ubiquitin-Protein Ligases* / metabolism

Substances

  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • Repressor Proteins
  • dinG protein, E coli
  • Polycomb Repressive Complex 1
  • RNF2 protein, human
  • Rnf2 protein, mouse
  • Ubiquitin-Protein Ligases