Phosphorylation of serine residues is fundamental for the calcium-binding ability of Orchestin, a soluble matrix protein from crustacean calcium storage structures

Arnaud Hecker, Olivier Testenière, Frédéric Marin, Gilles Luquet, Gianni Cesareni

Research output: Contribution to journalArticlepeer-review

Abstract

Orchestia cavimana is a terrestrial crustacean, which cyclically stores calcium in diverticula of the midgut, in the form of calcified amorphous concretions. These concretions are associated with a proteinaceous matrix, the main constituent of the soluble matrix is Orchestin, an acidic calcium-binding protein [Testenière et al., Biochem. J. 361 (2002) 327-335]. In the present paper, we clearly demonstrate that Orchestin is phosphorylated on serine and tyrosine residues, but that calcium binding only occurs via the phosphoserine residues. To our knowledge, this is the first example of an invertebrate mineralization for which a post-translational modification is clearly related to an important function of a calcifying protein.

Original languageEnglish
Pages (from-to)49-54
Number of pages6
JournalFEBS Letters
Volume535
Issue number1-3
DOIs
Publication statusPublished - Jan 30 2003

Keywords

  • Biomineralization
  • Calcium binding
  • Crustacean
  • Organic matrix
  • Phosphorylation

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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