Cellular and Molecular Life Sciences

, Volume 66, Issue 14, pp 2205–2218

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

Authors

  • Anne Berna
    • Institut de Biologie Moléculaire des Plantes du CNRS, Institut de BotaniqueUniversité de Strasbourg
  • François Bernier
    • Institut de Biologie Moléculaire des Plantes du CNRS, Institut de BotaniqueUniversité de Strasbourg
  • Eric Chabrière
    • Architecture et Fonction des Macromolécules BiologiquesCNRS, Université de la Méditerranée
  • Mikael Elias
    • Architecture et Fonction des Macromolécules BiologiquesCNRS, Université de la Méditerranée
    • School of Biological SciencesUniversity of Auckland
  • Andrew Suh
    • School of Biological SciencesUniversity of Auckland
Review

DOI: 10.1007/s00018-009-0006-6

Cite this article as:
Berna, A., Bernier, F., Chabrière, E. et al. Cell. Mol. Life Sci. (2009) 66: 2205. doi:10.1007/s00018-009-0006-6

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.

Keywords

DING protein Phosphate-binding protein Phosphate deprivation Pathogenesis Transcriptional modulation Bacteria Eukaryotes

Supplementary material

18_2009_6_MOESM1_ESM.tif (11.7 mb)
Supplementary Figure 1 (TIFF 12,024 kb)
18_2009_6_MOESM2_ESM.doc (37 kb)
Supplementary Figure 1: DING sequence alignment (DOC 37 kb)

Copyright information

© Birkhäuser Verlag, Basel/Switzerland 2009