Journal ArticleDOI
Receptor Protein Tyrosine Phosphatases in Nervous System Development
Karl G. Johnson,David Van Vactor +1 more
TLDR
Focusing on the roles RPTPs play in the development of the central nervous system, this review discusses how the elucidation of RPTP crystal structures, the biochemical analysis of phosphatase enzyme catalysis, and the characterization of complex signal transduction cascades downstream of RP TPs have generated testable models ofRPTP structure and function.Abstract:
Receptor protein tyrosine phosphatases (RPTPs) are key regulators of neuronal morphogenesis in a variety of different vertebrate and invertebrate systems, yet the mechanisms by which these proteins regulate central nervous system development are poorly understood. In the past few years, studies have begun to outline possible models for RPTP function by demonstrating in vivo roles for RPTPs in axon outgrowth, guidance, and synaptogenesis. In addition, the crystal structures of several RPTPs have been solved, numerous downstream effectors of RPTP signaling have been identified, and a small number of RPTP ligands have been described. In this review, we focus on how RPTPs transduce signals from the extracellular environment to the cytoplasm, using a detailed comparative analysis of the different RPTP subfamilies. Focusing on the roles RPTPs play in the development of the central nervous system, we discuss how the elucidation of RPTP crystal structures, the biochemical analysis of phosphatase enzyme catalysis, and the characterization of complex signal transduction cascades downstream of RPTPs have generated testable models of RPTP structure and function.read more
Citations
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Journal ArticleDOI
PTPσ Is a Receptor for Chondroitin Sulfate Proteoglycan, an Inhibitor of Neural Regeneration
Yingjie Shen,Alan P. Tenney,Sarah A. Busch,Kevin P. Horn,Fernando X. Cuascut,Kai Liu,Zhigang He,Jerry Silver,John G. Flanagan +8 more
TL;DR: It is shown that a transmembrane protein tyrosine phosphatase, PTPσ, binds with high affinity to neural CSPGs and may provide new therapeutic approaches to neural regeneration.
Journal ArticleDOI
Protein-tyrosine phosphatases and cancer
TL;DR: An improved understanding of how tyrosine phosphorylation function and how they are regulated might aid the development of new anticancer agents.
Journal ArticleDOI
Chromogenic/Fluorogenic Ensemble Chemosensing Systems.
TL;DR: This work has shown the ability of laser-spot assisted, 3D image analysis to characterize the geometry of the Tournaisian crystal and provide the CSM target with high precision.
Journal ArticleDOI
Proteoglycan-Specific Molecular Switch for RPTPσ Clustering and Neuronal Extension
C.H. Coles,Yingjie Shen,Alan P. Tenney,Alan P. Tenney,Christian Siebold,Geoffrey C. Sutton,W. Lu,John T. Gallagher,E. Yvonne Jones,John G. Flanagan,A. Radu Aricescu +10 more
TL;DR: It is reported that RPTPσ acts bimodally in sensory neuron extension, mediating CSPG inhibition and HSPG growth promotion, and leads to a model where proteoglycans can exert opposing effects on neuronal extension by competing to control the oligomerization of a common receptor.
Journal ArticleDOI
LAR receptor protein tyrosine phosphatases in the development and maintenance of excitatory synapses
Anthone W. Dunah,Emily Hueske,Michael Wyszynski,Michael Wyszynski,Casper C. Hoogenraad,Jacek Jaworski,Daniel T.S. Pak,Daniel T.S. Pak,Alyson Simonetta,Guosong Liu,Morgan Sheng +10 more
TL;DR: It is proposed that the cadherin-β-catenin complex is cotransported with AMPA receptors to synapses and dendritic spines by a mechanism that involves binding of liprin-α to LAR-RPTP and tyrosine dephosphorylation by LAR- RPTP.
References
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Transforming gene product of Rous sarcoma virus phosphorylates tyrosine
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Reversible Oxidation and Inactivation of Protein Tyrosine Phosphatases In Vivo
TL;DR: The results indicate that SHP-2 inhibits PDGFR signaling and suggest a mechanism by which autophosphorylation of the PDG FR occurs despite its association with SHp-2, which is shown to be transient oxidation of the SH2 domain containing PTP.
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Distinct morphogenetic functions of similar small GTPases: Drosophila Drac1 is involved in axonal outgrowth and myoblast fusion.
TL;DR: Cloned Drosophila homologs of rac and CDC42, Drac1, and Dcdc42 proteins cause qualitatively distinct morphological defects, suggesting that similar GTPases in the same subfamily have unique roles in morphogenesis.
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Slit is the midline repellent for the robo receptor in Drosophila.
TL;DR: Genetic evidence that Slit is the midline Robo ligand is presented and biochemical evidence thatSlit binds Robo is presented, suggesting that slit and robo display dosage-sensitive genetic interactions, indicating that they function in the same pathway.