PTPRE

PTPRE

PTPRE: Human Protein Receptor Tyrosine Phosphatase E
PDB Code: 2JJD
Description
PTPRE belongs, together with RPTPA, to the receptor class 4 subfamily of protein-tyrosine phosphatases. Members of this phosphatase family contain a short extracellular domain, a single transmembrane region, and two tandem cytoplasmic catalytic domains (D1 and D2 domain). In addition to the transmembrane form of PTPRE, four cytoplasmic variants (cyt PTPepsilon, p67, p65, cyt-PTPepsilonPD1) lacking the extracellular and membrane spanning domains have been described.
PTPRE is involved in regulation of a variety of signaling pathways including voltage-gated potassium channel activity, negative regulation of insulin-receptor and JAK/STAT signaling. A role of PTPRE in osteoclast and macrophage function, regulation of cerebellar development as well as in suppression of endothelial cell proliferation has also been described.
PTPRE is highly expressed in leukocytes, particularly in monocytes and granulocytes, but moderate expression levels have been detected in most organs. PTPRE mRNA is detected in the neural tube of day 12 postcoitum embryo and in the nervous system including brain and spinal cord, whereas in neonatal mice expression is widely distributed in the central nervous system with strongest expression in the hippocampus, cerebral cortex, and olfactory bulb. In addition, PTPRE expression is significantly elevated in mouse mammary tumours.
PTPRE-/- mice show acute delay in myelination of Schwann cells and enhanced phosphorylation and conductance of voltage-gated potassium channels. Female knockout mice also exhibit increased trabecular bone mass due to cell-specific defects in osteoclast function. Transgenic mice overexpressing PTPRE in mammary epithelium develop pronounced and persistent mammary hyperplasia accompanied by residual milk production and solitary mammary tumours are often detected secondary to mammary hyperplasia.
ere we determined the structure of both PTPRE catalytic domains at 3.2 Å resolution. The quality of the refined structure was significantly improved by use of six-fold non-crystallographic symmetry averaging of the electron density maps to aid model building, resulting in a high quality three dimensional model of this interesting enzyme.

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