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Protein tyrosine phosphatase, receptor type, S

RPTPs, RPTPsigma, Ptprs, PTPsigma
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an extracellular region, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. The extracellular region of this protein is composed of multiple Ig-like and fibronectin type III-like domains. Studies of the similar gene in mice suggested that this PTP may be involved in cell-cell interaction, primary axonogenesis, and axon guidance during embryogenesis. This PTP has been also implicated in the molecular control of adult nerve repair. Four alternatively spliced transcript variants, which encode distinct proteins, have been reported. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: LAR, CAN, Pts, fibronectin, CD45
Papers on RPTPs
Developmental expression and function analysis of protein tyrosine phosphatase receptor type D in oligodendrocyte myelination.
Qiu et al., Louisville, United States. In Neuroscience, Dec 2015
Receptor protein tyrosine phosphatases (RPTPs) are extensively expressed in the central nervous system (CNS), and have distinct spatial and temporal patterns in different cell types during development.
Protein tyrosine phosphatase receptor S acts as a metastatic suppressor in hepatocellular carcinoma by control of epithermal growth factor receptor-induced epithelial-mesenchymal transition.
Fan et al., Shanghai, China. In Hepatology, Oct 2015
In this study, we report that protein tyrosine phosphatase receptor S (PTPRS) is significantly down-regulated in nearly 80% of HCCs, and its expression negatively correlates with aggressive pathological features, such as larger tumor size and advanced stage.
Splicing-Dependent Trans-synaptic SALM3-LAR-RPTP Interactions Regulate Excitatory Synapse Development and Locomotion.
Kim et al., Taejŏn, South Korea. In Cell Rep, Oct 2015
Here, we identify an interaction between SALM3 and LAR family receptor protein tyrosine phosphatases (LAR-RPTPs) that requires the mini-exon B splice insert in LAR-RPTPs.
The R3 receptor-like protein tyrosine phosphatase subfamily inhibits insulin signalling by dephosphorylating the insulin receptor at specific sites.
Noda et al., Okazaki, Japan. In J Biochem, Sep 2015
The R3 subfamily (Ptprb, Ptprh, Ptprj and Ptpro) of receptor-like protein tyrosine phosphatases (RPTPs) is characterized by an extracellular region with 6-17 fibronectin type III-like repeats and a cytoplasmic region with a single phosphatase domain.
Protein Tyrosine Phosphatase PTPRS Is an Inhibitory Receptor on Human and Murine Plasmacytoid Dendritic Cells.
Reizis et al., New York City, United States. In Immunity, Sep 2015
We report that within the human immune system, receptor protein tyrosine phosphatase sigma (PTPRS) is expressed specifically on pDCs.
Extracellular regulation of type IIa receptor protein tyrosine phosphatases: mechanistic insights from structural analyses.
Aricescu et al., Bonn, Germany. In Semin Cell Dev Biol, 2015
The receptor protein tyrosine phosphatases (RPTPs) exhibit a wide repertoire of cellular signalling functions.
RPTPs in axons, synapses and neurology.
Stoker, London, United Kingdom. In Semin Cell Dev Biol, 2015
Receptor-like protein tyrosine phosphatases represent a large protein family related to cell adhesion molecules, with diverse roles throughout neural development in vertebrates and invertebrates.
Regulation of development and cancer by the R2B subfamily of RPTPs and the implications of proteolysis.
Brady-Kalnay et al., Cleveland, United States. In Semin Cell Dev Biol, 2015
The initial cloning of receptor protein tyrosine phosphatases (RPTPs) was met with excitement because of their hypothesized function in counterbalancing receptor tyrosine kinase signaling.
R3 receptor tyrosine phosphatases: conserved regulators of receptor tyrosine kinase signaling and tubular organ development.
Zinn et al., Pasadena, United States. In Semin Cell Dev Biol, 2015
R3 receptor tyrosine phosphatases (RPTPs) are characterized by extracellular domains composed solely of long chains of fibronectin type III repeats, and by the presence of a single phosphatase domain.
Integrated methylome and transcriptome analysis reveals novel regulatory elements in pediatric acute lymphoblastic leukemia.
Taylor et al., Columbia, United States. In Epigenetics, 2014
These genes include potential epi-driver genes, such as SYNE1, PTPRS, PAWR, HDAC9, RGCC, MCOLN2, LYN, TRAF3, FLT1, and MELK, which may provide a selective advantage to leukemic cells.
LAR-RPTPs: synaptic adhesion molecules that shape synapse development.
Ko et al., Seoul, South Korea. In Trends Cell Biol, 2013
Leukocyte common antigen-related receptor protein tyrosine phosphatases (LAR-RPTPs) have previously been implicated as essential elements in central nervous system (CNS) development.
Receptor protein tyrosine phosphatase sigma regulates synapse structure, function and plasticity.
Kennedy et al., Montréal, Canada. In J Neurochem, 2012
The results of this study demonistrated that RPTPsigma limits synapse number and regulates synapse structure and function in the mature central nervous system.
The cytokine midkine and its receptor RPTPζ regulate B cell survival in a pathway induced by CD74.
Shachar et al., Israel. In J Immunol, 2012
The cytokine midkine and its receptor RPTPzeta regulate B cell survival in a pathway induced by CD74.
Structural insights into the homology and differences between mouse protein tyrosine phosphatase-sigma and human protein tyrosine phosphatase-sigma.
Li et al., Shanghai, China. In Acta Biochim Biophys Sin (shanghai), 2011
Structural insights into the homology and differences between mouse protein tyrosine phosphatase-sigma and human protein tyrosine phosphatase-sigma.
Receptor-like tyrosine phosphatases CD45 and CD148 have distinct functions in chemoattractant-mediated neutrophil migration and response to S. aureus.
Weiss et al., San Francisco, United States. In Immunity, 2011
Tyrosine phosphorylation pathways and receptor-like tyrosine phosphatases (RPTPs) are rarely considered in chemoattractant-mediated GPCR signaling.
Genomic dissection of the epidermal growth factor receptor (EGFR)/PI3K pathway reveals frequent deletion of the EGFR phosphatase PTPRS in head and neck cancers.
Chan et al., New York City, United States. In Proc Natl Acad Sci U S A, 2011
Intragenic microdeletions of the EGFR phosphatase PTPRS were found frequently (26%) in head and neck cancers, identifying this gene as a target of 19p13 loss.
Protein tyrosine phosphatase σ regulates the synapse number of zebrafish olfactory sensory neurons.
Mishina et al., Tokyo, Japan. In J Neurochem, 2011
Transgenic zebrafish carrying a promoter-driven expression vector reveal the increased density of olfactory sensory neuron-specific cell synapses.
PTPsigma is a receptor for chondroitin sulfate proteoglycan, an inhibitor of neural regeneration.
Flanagan et al., Boston, United States. In Science, 2009
PTPsigma binds with high affinity to neural chondroitin sulfate proteoglycans(CPSGs); binding involves chondroitin sulfate chains & a specific site on 1st immunoglobulin-like domain of PTPsigma; results indicate PTPsigma can act as a receptor for CSPGs
Nonreceptor protein-tyrosine phosphatases in immune cell signaling.
Neel et al., Boston, United States. In Annu Rev Immunol, 2006
Genome sequencing efforts have revealed a large and diverse superfamily of PTPs, which can be subdivided into receptor-like (RPTPs) and nonreceptor (NRPTPs).
Inhibition of netrin-mediated axon attraction by a receptor protein tyrosine phosphatase.
Tessier-Lavigne et al., Stanford, United States. In Science, 2004
The known effects of other RPTPs in axon guidance could result from modulation of guidance receptors like UNC-40/DCC.
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