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Tyrosine phosphatases as regulators of skeletal development and metabolism
Author(s) -
Schiller Katherine R.,
Mauro Laura J.
Publication year - 2005
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.20515
Subject(s) - protein tyrosine phosphatase , phosphorylation , dephosphorylation , biology , tyrosine , tyrosine phosphorylation , protein phosphorylation , signal transduction , microbiology and biotechnology , biochemistry , kinase , phosphatase , cell signaling , receptor tyrosine kinase , sh2 domain , protein kinase a
The protein tyrosine kinases (PTK) and the protein tyrosine phosphatases (PTPs) are enzymes which play an integral role in tyrosine phosphorylation‐dependent signaling cascades. By catalyzing the phosphorylation and dephosphorylation of cellular proteins, these enzymes direct the steady‐state levels of specific phosphoproteins and ultimately dictate the functional state of all cells. The importance of this type of signaling in the skeleton is accepted but poorly understood. The contribution of the PTKs to signaling events in bone has been well studied but, in contrast, the regulation by PTPs is poorly defined. The recent identification of 107 genes within the human genome which encode members of the PTP superfamily emphasizes the need to consider the importance of these proteins in skeletal tissue. In this prospective, we will summarize the present state of our knowledge regarding the function of this enzyme superfamily, illustrating its relevance to the development and maintenance of the skeleton and highlighting future directions that should improve our understanding of these critical signaling molecules. © 2005 Wiley‐Liss, Inc.