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The roles of autophosphorylation and phosphorylation in the life of osteopontin
Author(s) -
Saavedra Raul A.
Publication year - 1994
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.950161210
Subject(s) - osteopontin , autophosphorylation , phosphoprotein , phosphorylation , serine , kinase , biochemistry , chemistry , microbiology and biotechnology , phosphoserine , threonine , protein phosphorylation , biology , protein kinase a , immunology
Osteopotin 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 extracelluar 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.