TY - JOUR
T1 - The roles of protein tyrosine phosphatases in bone-resorbing osteoclasts
AU - Shalev, Moran
AU - Elson, Ari
N1 - We apologize to many colleagues whose work could not be cited due to strict space limitations. We thank Dr. Ester Feldmesser of the Weizmann Institute of Science for assistance with analysis of RNAseq data. This study was supported by the Kekst Family Center for Medical Genetics at the Weizmann Institute of Science, and by the Gutwirth Foundation (to AE). AE is the incumbent of the Marshall and Renette Ezralow Professorial Chair.
PY - 2019/1
Y1 - 2019/1
N2 - Maintaining the proper balance between osteoblast-mediated production of bone and its degradation by osteoclasts is essential for health. Osteoclasts are giant phagocytic cells that are formed by fusion of monocyte-macrophage precursor cells; mature osteoclasts adhere to bone tightly and secrete protons and proteases that degrade its matrix. Phosphorylation of tyrosine residues in proteins, which is regulated by the biochemically antagonistic activities of protein tyrosine kinases and protein tyrosine phosphatases (PTPs), is central in regulating the production of osteoclasts and their bone-resorbing activity. Here we review the roles of individual PTPs of the classical and dual-specificity sub-families that are known to support these processes (SHP2, cyt-PTPe, PTPRO, PTP-PEST, CD45) or to inhibit them (SHP1, PTEN, MKP1). Characterizing the functions of PTPs in osteoclasts is essential for complete molecular level understanding of bone resorption and for designing novel therapeutic approaches for treating bone disease.
AB - Maintaining the proper balance between osteoblast-mediated production of bone and its degradation by osteoclasts is essential for health. Osteoclasts are giant phagocytic cells that are formed by fusion of monocyte-macrophage precursor cells; mature osteoclasts adhere to bone tightly and secrete protons and proteases that degrade its matrix. Phosphorylation of tyrosine residues in proteins, which is regulated by the biochemically antagonistic activities of protein tyrosine kinases and protein tyrosine phosphatases (PTPs), is central in regulating the production of osteoclasts and their bone-resorbing activity. Here we review the roles of individual PTPs of the classical and dual-specificity sub-families that are known to support these processes (SHP2, cyt-PTPe, PTPRO, PTP-PEST, CD45) or to inhibit them (SHP1, PTEN, MKP1). Characterizing the functions of PTPs in osteoclasts is essential for complete molecular level understanding of bone resorption and for designing novel therapeutic approaches for treating bone disease.
UR - http://www.scopus.com/inward/record.url?scp=85050375260&partnerID=8YFLogxK
U2 - https://doi.org/10.1016/j.bbamcr.2018.07.005
DO - https://doi.org/10.1016/j.bbamcr.2018.07.005
M3 - مقالة مرجعية
SN - 0167-4889
VL - 1866
SP - 114
EP - 123
JO - Biochimica Et Biophysica Acta-Molecular Cell Research
JF - Biochimica Et Biophysica Acta-Molecular Cell Research
IS - 1
ER -