Receptor protein tyrosine phosphatase

Tertoolen, L. G., Blanchetot, C., Jiang, G., Overvoorde, J., Gadella, T. W., Jr., Hunter, T. and den Hertog, J. (2001). Dimerization of receptor protein-tyrosine phosphatase alpha in living cells. BMC Cell Biol. 2, 8. 

Majeti, R. and Weiss, A. (2001). Regulatory mechanisms for receptor protein tyrosine phosphatases. Chem. Rev. 101, 2441-2448. 

Brady-Kalnay, S., Rimm, D. and Tonks, N. Receptor protein tyrosine phosphatase PTPm associates with cadherins and catenins in vivo. J. Cell Biol. 130 977-986,1995. 

Receptor protein tyrosine phosphatases consist of an extracellular domain, a transmembrane domain and one or two intracellular catalytic domains 426... 

FIGURE 24-10 Schematic structures of nonreceptor protein tyrosine phosphatases (NRPTPs) and receptor protein tyrosine phosphatases (RPTPs). NRPTPs contain a catalytic domain and various regulatory domains. RPTPs are composed of an extracellular domain, a transmembrane domain and an intracellular domain with one or two catalytic domains. Like receptor protein tyrosine kinases, the structural features of the extracellular domains divide the RPTPs into different families. (With permission from reference [12]). 

Majeti, R., Bilwes, A. M., Noel, J. P. et al. Dimerization-induced inhibition of receptor protein tyrosine phosphatase function through an inhibitory wedge. Science 279 88-91,1998. 

Aicher B, Lerch MM, Muller T et al (1997) Cellular redistribution of protein tyrosine phosphatases LAR and PTPa by inducible proteolytic processing. J Cell Biol 138 681-96 Alete DE, Weeks ME, Hovanession AG et al (2006) Cell surface nucleolin on developing muscle is a potential ligand for the axonal receptor protein tyrosine phosphatase-cr. FEBS J 273 4668-81 Andrade MA, Perez-Iratxeta C, Ponting CP (2001) Protein repeats structures, functions, and evolution. J Struct Biol 134 117-31... 

Krasnoperov VG, Beavis R, Chepumy OG et al (1996) The calcium-independent receptor of a-latrotoxin is not a neurexin. Biochem Biophys Res Commun 227 868-75 Krasnoperov VG, Bittner MA, Beavis R et al (1997) a-Latrotoxin stimulates exocytosis by the interaction with a neuronal G-protein-coupled receptor. Neuron 18 925-37 Krasnoperov VG, Bittner MA, Mo W et al (2002b) Protein tyrosine phosphatase-G is a novel member of the functional family of a-latrotoxin receptors. J Biol Chem 277 35887-95 Kreienkamp HJ, Zitzer H, Gundelfinger ED et al (2000) The calcium-independent receptor for a-latrotoxin from human and rodent brains interacts with members of the ProSAP/SSTRIP/Shank family of multidomain proteins. J Biol Chem 275 32387-90 Lajus S, Lang J (2006) Splice variant 3, but not 2 of receptor protein-tyrosine phosphatase a can mediate stimulation of insulin-secretion by a-latrotoxin. J Cell Biochem 98 1552-9 Lajus S, Vacher P, Huber D et al (2006) a-Latrotoxin induces exocytosis by inhibition of voltage-dependent K+ channels and by stimulation of L-type Ca2+ channels via latrophilin in [5-cells. J Biol Chem 281 5522-31... 

Thompson KM, Uetani N, Manitt C et al (2003) Receptor protein tyrosine phosphatase sigma inhibits axonal regeneration and the rate of axon extension. Mol Cell Neurosci 23 681-92 Tobaben S, Sfldhof TC, Stahl B (2002) Genetic analysis of a-latrotoxin receptors reveals functional interdependence of CIRL/latrophilin 1 and neurexin la. J Biol Chem 277 6359-65 Tobaben S, Sfldhof TC, Stahl B (2000) The G protein-coupled receptor CL1 interacts directly with proteins of the Shank family. J Biol Chem 275 36204-10 Tonks NK (2006) Protein tyrosine phosphatases from genes, to function, to disease. Nat Rev Mol Cell Biol 7 833 16... 

Ratcliffe CF, Qu Y, McCormick KA et al 2000 A sodium channel signaling complex modulation by associated receptor protein tyrosine phosphatase beta. Nat Neurosci 3 437-444... 

Proteins do not need to be metalloproteins to interact with cadmium, and the proteins with reactive cysteines described in Section 4.2.1 are examples of non-metalloproteins interacting with cadmium. In addition, some proteins that are not recognized as metalloproteins bind zinc extremely tightly. For example, the cytoplasmic domain of receptor protein tyrosine phosphatase p binds zinc with a value of 27 pM [109]. Cadmium is expected to bind tightly to these sites. Significantly, the widespread use of CdCl2 in crystallization studies, to prepare heavy metal derivatives and to phase the diffraction data, provides hundreds of protein structures in which Cd " interacts with amino-acid residues, often in positions that are not known to bind cations. 

A., and Papadimitriou, E. (2009). Nitric oxide stimulates migration of human endothelial and prostate cancer cells through up-regulation of pleiotrophin expression and its receptor protein tyrosine phosphatase beta/zeta. Int. J. Cancer 124, 1785-1793. 

---