The roles of autophosphorylation and phosphorylation in the life of osteopontin.
Osteopontin is a secreted glycosylated phosphoprotein found in bone and other normal and malignant tissues. Osteopontin can be autophosphorylated on tyrosine residues and can also be phosphorylated on serine and threonine residues by several protein kinases. Autophosphorylation of osteopontin may generate sites for specific interactions with other proteins on the cell surface and/or within the extracellular matrix. These interactions of osteopontin are thought to be essential for bone mineralization and function. The polyaspartic acid motif of osteopontin, in combination with neighboring sequences that include serine residues phosphorylated by protein kinases, could fold and assemble into a molecular structure that participates in the mineralization of the bone matrix.
Department of Orthopaedic Surgery, Harvard Medical School, Boston, MA.
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Saavedra
D000818:Animals; D002118:Calcium / Q000378:metabolism; D006801:Humans; D053495:Osteopontin; D010766:Phosphorylation; D011485:Protein Binding; D011494:Protein Kinases / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D012795:Sialoglycoproteins / Q000378:metabolism*
D011994:Recombinant Proteins; C506895:SPP1 protein, human; D012795:Sialoglycoproteins; D053495:Osteopontin; D011494:Protein Kinases; D002118:Calcium