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- Title
Phosphorylation of serine residues is fundamental for the calcium-binding ability of Orchestin, a soluble matrix protein from crustacean calcium storage structures
- Authors
Hecker, Arnaud; Testenière, Olivier; Marin, Frédéric; Luquet, Gilles
- 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 [Testenie`re 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.
- Subjects
PHOSPHORYLATION; BIOMINERALIZATION; CRUSTACEA
- Publication
FEBS Letters, 2003, Vol 535, Issue 1-3, p49
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(02)03856-5