Published 6 issues per year
ISSN Print: 1045-4403
ISSN Online: 2162-6502
Indexed in
Protein Tyrosine Phosphatases in Osteoclasts
ABSTRACT
Osteoclasts are large cells derived from the monocyte-macrophage hematopoietic cell lineage, whose primary function is to degrade bone in various physiological contexts. Reversible phosphorylation of tyrosine residues in proteins is known to play significant roles in regulating the function of osteoclasts, much as it does in other cell types. Protein tyrosine phosphatases (PTPs) are among the major regulators of this process, but significant gaps exist in our knowledge of which phosphatases function in osteoclasts and the nature of their precise cellular and molecular roles. We review here the roles of the four tyrosine phosphatases that are known currently to be expressed in osteoclastsPTPRO, PTP epsilon (PTPε), SHP-1, and PTP-PEST. Of these, PTPRO and PTPε support osteoclast activity, whereas SHP-1 inhibits it. Much future research is required to uncover additional PTPs that function in osteoclasts and provide full molecular-level accounting of their respective roles in osteoclasts.
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Lau Kin-Hing William, Sheng Matilda H.-C., A novel miR17 /protein tyrosine phosphatase-oc/EphA4 regulatory axis of osteoclast activity, Archives of Biochemistry and Biophysics, 650, 2018. Crossref
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Lountos George T., Raran-Kurussi Sreejith, Zhao Bryan M., Dyas Beverly K., Burke Terrence R., Ulrich Robert G., Waugh David S., High-resolution crystal structures of the D1 and D2 domains of protein tyrosine phosphatase epsilon for structure-based drug design, Acta Crystallographica Section D Structural Biology, 74, 10, 2018. Crossref