Receptor tyrosine phosphatase

Receptor/nonreceptor phosphatases Receptor tyrosine phosphatases CD45, LAR... 

Ratcliffe CF, Qu Y, McCormick KA, Tibbs VC, Dixon JE, Scheuer T, Cat-terall WA. A sodium channel signaling complex modulation by associated receptor tyrosine phosphatase beta. Nature Neurosci 2000 3 437-444. 

Desai, D. M., Sap, J., Schlessinger, J. et al. Ligand-mediated negative regulation of a chimeric transmembrane receptor tyrosine phosphatase. Cell 73 541-554,1993. 

Peles, E., Nativ, M., Campbell, P.L., Sakurai, T., Martinez, R., Lev, S., Clary, D.O., Schilling, I, Barnea, G. and Plowman, G.D. The carbonic acid anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition molecule contactin (1995) Cell 82, 251-260... 

Phosphotyrosine phosphatases are only one of several classes of phosphatases. It has been estimated that about a thousand phosphatases of different specificities exist. Here, we consider only cytosolic and receptor tyrosine phosphatases (Fig. 3.8) (phosphoserine/threonine phosphatases are discussed in Chapter 7). 

The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal ceU recognition molecule contactin. CeU 82 251-260. 

Zondag GC, Koningstein GM, Jiang YP, Sap J, Moolenaar WH, et al. 1995. Homophilic interactions mediated by receptor tyrosine phosphatases mu and kappa. A critical role for the novel extracellular MAM domain [published erratum appears in J Biol Chem 1995 Oct 13 270(41) 24621]. J Biol Chem 270 14247-14250. 

The receptor-like protein tyrosine phosphatases have a transmembrane and, in some cases, a large extracellular domain with a very variable structure (Fig. 8.19). Many, but not all, membrane protein tyrosine phosphatases have two catalytic domains in the cytoplasmic region. The overall structure is very similar to the structure of transmembrane receptors. Only recently, cellular ligands for receptor tyrosine phosphatases have been identified that function as their specific regulators. The receptor tyrosine phosphatase C has been found to be specifically inhibited by pleiotrophin, which is a cytokine implicated in tumor angiogenesis. Several studies have demonstrated a role for receptor PTPs in neuronal cell adhesion signaling pathways. In cells of the neural tissue, a surface protein, contactin, has been identified as an extracellular ligand of PTPa. 

Desai, C.J., Popova, E. and Zinn, K. (1994) A Drosophila receptor tyrosine phosphatase expressed in the embryonic CNS and larval optic lobes is a member of the set of proteins bearing the "HRP carbohydrate epitope. J. Neurosci. 14 7272-7283. 

Barnea, G., Grumet, M., Milev, P., Silvennoinen, O., Levy, J.B., Sap, J. and Schlessinger, J. (1994) Receptor tyrosine phosphatase beta is expressed in the form of proteoglycan and binds to the extracellular matrix protein tenascin. J. Biol. Chem. 269 14349-14352. 

Jeon, M. Zinn, K. (2009). Receptor tyrosine phosphatases control tracheal tube geometries through negative regulation of Egfr signaling. Development 136,3121-3129. 

The receptor tyrosine phosphatase-like protein islet cell autoantigen 512 binds the protein domain named for PSD-95, disc large and ZO-1 domains of P2-synthrophin and nNOS in pancreatic B cells (Ort et al. 2000). 

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