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

FEBS Letters

Luquet, Gilles²  Marin, Frédéric¹  Hecker, Arnaud²  Testenière, Olivier² 

[1] IsoTis, Prof. Bronkhorstlaan, 10, Gebouw D, 3723 MB Bilthoven, The Netherlands;UMR CNRS 5548, Développement-Communication chimique, Université de Bourgogne, 6 Bd Gabriel, F-21000 Dijon, France

关键词: Biomineralization;    Calcium binding;    Crustacean;    Organic matrix;    Phosphorylation;   

DOI  :  10.1016/S0014-5793(02)03856-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown