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https://www.readbyqxmd.com/read/25385546/structural-basis-for-extracellular-cis-and-trans-rptp%C3%AF-signal-competition-in-synaptogenesis
#1
Charlotte H Coles, Nikolaos Mitakidis, Peng Zhang, Jonathan Elegheert, Weixian Lu, Andrew W Stoker, Terunaga Nakagawa, Ann Marie Craig, E Yvonne Jones, A Radu Aricescu
Receptor protein tyrosine phosphatase sigma (RPTPσ) regulates neuronal extension and acts as a presynaptic nexus for multiple protein and proteoglycan interactions during synaptogenesis. Unknown mechanisms govern the shift in RPTPσ function, from outgrowth promotion to synaptic organization. Here, we report crystallographic, electron microscopic and small-angle X-ray scattering analyses, which reveal sufficient inter-domain flexibility in the RPTPσ extracellular region for interaction with both cis (same cell) and trans (opposite cell) ligands...
November 11, 2014: Nature Communications
https://www.readbyqxmd.com/read/19573017/dimerization-of-tyrosine-phosphatase-ptpro-decreases-its-activity-and-ability-to-inactivate-trkc
#2
COMPARATIVE STUDY
Amy E Hower, Pedro J Beltran, John L Bixby
Receptor-protein tyrosine phosphatases (RPTPs), like receptor tyrosine kinases, regulate neuronal differentiation. While receptor tyrosine kinases are dimerized and activated by extracellular ligands, the extent to which RPTPs dimerize, and the effects of dimerization on phosphatase activity, are poorly understood. We have examined a neuronal type III RPTP, PTPRO; we find that PTPRO can form dimers in living cells, and that disulfide linkages in PTPROs intracellular domain likely regulate dimerization. Dimerization of PTPROs transmembrane and intracellular domains, achieved by ligand binding to a chimeric fusion protein, decreases activity toward artificial peptides and toward a putative substrate, tropomyosin-related kinase C (TrkC)...
September 2009: Journal of Neurochemistry
https://www.readbyqxmd.com/read/18477627/protein-tyrosine-phosphatase-receptor-type-z-dephosphorylates-trka-receptors-and-attenuates-ngf-dependent-neurite-outgrowth-of-pc12-cells
#3
Takafumi Shintani, Masaharu Noda
Protein tyrosine phosphatase receptor type Z (Ptprz/Ptpzeta/RPTPbeta) is a receptor-like protein tyrosine phosphatase (RPTP) which is predominantly expressed in the central nervous system. Tropomyosin-related kinases (Trks) are single-pass transmembrane molecules that are highly expressed in the developing nervous system. Upon the ligand binding of neurotrophins, Trk receptors are activated through autophosphorylation of tyrosine residues; however, the PTPs responsible for the negative regulation of Trk receptors have not been fully elucidated...
August 2008: Journal of Biochemistry
https://www.readbyqxmd.com/read/12532410/expression-of-ptpro-during-mouse-development-suggests-involvement-in-axonogenesis-and-differentiation-of-nt-3-and-ngf-dependent-neurons
#4
Pedro J Beltran, John L Bixby, Brian A Masters
Competition and cooperation between type II and type III receptor protein tyrosine phosphatases (RPTPs) regulate axon extension and pathfinding in Drosophila. The first step to investigate whether RPTPs influence axon growth in the more complex vertebrate nervous system is to identify which neurons express a particular RPTP. We studied the expression of mouse PTPRO, a type III RPTP with an extracellular region containing eight fibronectin type III domains, during embryogenesis and after birth. Mouse PTPRO mRNA is expressed exclusively in two cell types: neurons and kidney podocytes...
February 17, 2003: Journal of Comparative Neurology
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