| Modification Notes |
Protein tyrosine phosphatases (PTPs) and protein tyrosine kinases (PTKs) play an ubiquitous role in the regulation of tyrosine phosphorylation-mediated signaling pathways. Tyrosine-phosphorylated proteins can be dephosphorylated through the action of PTPs, which are likely to play a regulatory role in the control of cellular growth and differentiation. The gene encoding human PTP-PEST maps to chromosome 7q11.23 and encodes a 780 amino acid cytosolic nonreceptor protein. PTP-PEST is expressed abundantly in a wide variety of hemopoietic cell types, including B cells and T cells. PTP-PEST may constitutively associate with several signalling molecules, including Shc, paxillin, Csk and Cas. In addition, PTP-PEST can induce dephosphorylation of Shc, Pyk2, Fak and Cas, and inactivate the Ras pathway. Dephosphorylation of c-Abl by PTP-PEST represents a novel mechanism by which c-Abl activity is regulated. PTP-PEST can also influence cytoskeletal organization by promoting the turnover of focal adhesions required for cell migration, and through regulation of the proline, serine, threonine phosphatase interacting protein (PSTPIP)-mediated cleavage furrow formation or disassembly during normal cell division. |