The roles of autophosphorylation and phosphorylation in the life of osteopontin
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Abstract
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.Keywords
This publication has 48 references indexed in Scilit:
- Identification of Two Phosphorylation Motifs in Bovine OsteopontinBiochemical and Biophysical Research Communications, 1994
- Mouse Osteopontin Expressed in E. coli Exhibits Autophosphorylating Activity of Tyrosine ResiduesBiochemical and Biophysical Research Communications, 1993
- Prediction of Protein Secondary Structure at Better than 70% AccuracyJournal of Molecular Biology, 1993
- Ultrastructural immunolocalization of noncollagenous (osteopontin and osteocalcin) and plasma (albumin and α2HS-glycoprotein) proteins in rat boneJournal of Bone and Mineral Research, 1993
- In vitro Phosphorylation of Mouse Osteopontin Expressed in E. coliBiochemical and Biophysical Research Communications, 1993
- High‐resolution immunolocalization of osteopontin and osteocalcin in bone and cartilage during endochondral ossification in the chicken tibiaThe Anatomical Record, 1992
- Evidence for the formation of a complex between osteopontin and osteocalcinJournal of Bone and Mineral Research, 1992
- Secreted phosphoprotein mrna is induced during multi‐stage carcinogenesis in mouse skin and correlates with the metastatic potential of murine fibroblastsInternational Journal of Cancer, 1990
- Multiple forms of SppI (secreted phosphoprotein, osteopontin) synthesized by normal and transformed rat bone cell populations: Regulation by TGF-βBiochemical and Biophysical Research Communications, 1989
- Tissue specificity and developmental expression of rat osteopontinBiochemical and Biophysical Research Communications, 1987