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

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RESEARCH PRODUCT

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

Olivier Testenière Frédéric Marin Arnaud Hecker Gilles Luquet

subject

Biomineralization MESH: Amino Acid Sequence MESH: Calcium-Binding Proteins Matrix (biology)01 natural sciences Biochemistry Calcium in biology MESH: Tyrosine Serine chemistry.chemical_compound MESH: Structure-Activity Relationship Structural Biology Crustacea Serine Electrophoresis Gel Two-Dimensional MESH: Animals Tyrosine Phosphorylation 0303 health sciences Biochemistry MESH: Calcium Phosphorylation Electrophoresis Polyacrylamide Gel Organic matrix Protein Binding Molecular Sequence Data Biophysics chemistry.chemical_element Crustacean Calcium Biology 010402 general chemistry MESH: Calcification Physiologic 03 medical and health sciences Structure-Activity Relationship Calcification Physiologic MESH: Crustacea Genetics Animals MESH: Protein Binding [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Amino Acid Sequence MESH: Serine Molecular Biology 030304 developmental biology Calcium metabolism MESH: Molecular Sequence Data MESH: Phosphorylation Calcium-Binding Proteins Cell Biology MESH: Electrophoresis Gel Two-Dimensional 0104 chemical sciences chemistry Phosphoserine MESH: Protein Processing Post-Translational Tyrosine Calcium Calcium binding Protein Processing Post-Translational MESH: Electrophoresis Polyacrylamide Gel

description

International audience; 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.

year	journal	country	edition	language
2003-01-30

10.1016/s0014-5793(02)03856-5 https://hal.archives-ouvertes.fr/hal-03023835