The nuclear isoform of protein-tyrosine phosphatase TC-PTP regulates interleukin-6-mediated signaling pathway through STAT3 dephosphorylation (Q24308062)

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English	The nuclear isoform of protein-tyrosine phosphatase TC-PTP regulates interleukin-6-mediated signaling pathway through STAT3 dephosphorylation	scientific article

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The nuclear isoform of protein-tyrosine phosphatase TC-PTP regulates interleukin-6-mediated signaling pathway through STAT3 dephosphorylation (English)

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signal transducer and activator of transcription 3

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GOA release 2020-03-11

interleukin-6-mediated signaling pathway

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GOA release 2020-03-11

author name string

Tetsuya Yamamoto

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Yuichi Sekine

2

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Keiichi Kashima

3

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Atsuko Kubota

4

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Noriko Sato

5

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Naohito Aoki

6

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Tadashi Matsuda

7

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language of work or name

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publication date

4 October 2002

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Biochemical and Biophysical Research Communications

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297

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4

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811-7

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Interleukin-6 and its receptor: a paradigm for cytokines

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Signaling mechanisms through gp130: a model of the cytokine system

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Cytokine signal transduction

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Cytokine receptor signalling

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Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins

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Protein tyrosine phosphatases in signal transduction.

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Combinatorial control of the specificity of protein tyrosine phosphatases

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cDNA isolated from a human T-cell library encodes a member of the protein-tyrosine-phosphatase family

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Expression of a human T-cell protein-tyrosine-phosphatase in baby hamster kidney cells

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Cloning and characterization of a mouse cDNA encoding a cytoplasmic protein-tyrosine-phosphatase

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Nuclear localization and cell cycle regulation of a murine protein tyrosine phosphatase

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Cellular stress regulates the nucleocytoplasmic distribution of the protein-tyrosine phosphatase TCPTP.

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Impaired bone marrow microenvironment and immune function in T cell protein tyrosine phosphatase-deficient mice

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A cytosolic protein-tyrosine phosphatase PTP1B specifically dephosphorylates and deactivates prolactin-activated STAT5a and STAT5b

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A nuclear protein tyrosine phosphatase TC-PTP is a potential negative regulator of the PRL-mediated signaling pathway: dephosphorylation and deactivation of signal transducer and activator of transcription 5a and 5b by TC-PTP in nucleus

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A central role for Stat3 in IL-6-induced regulation of growth and differentiation in M1 leukemia cells

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Cross-talk between signal transducer and activator of transcription 3 and estrogen receptor signaling

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Plat-E: an efficient and stable system for transient packaging of retroviruses

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SOCS-1 can suppress CD3zeta- and Syk-mediated NF-AT activation in a non-lymphoid cell line

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Physical interaction between epidermal growth factor receptor and DNA-dependent protein kinase in mammalian cells

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Interleukin-6 triggers the association of its receptor with a possible signal transducer, gp130

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Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase

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A family of cytokine-inducible inhibitors of signalling

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A new protein containing an SH2 domain that inhibits JAK kinases

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Structure and function of a new STAT-induced STAT inhibitor

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Specific inhibition of Stat3 signal transduction by PIAS3

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Protein tyrosine phosphatase 2 (SHP-2) moderates signaling by gp130 but is not required for the induction of acute-phase plasma protein genes in hepatic cells

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Activation of the protein tyrosine phosphatase SHP2 via the interleukin-6 signal transducing receptor protein gp130 requires tyrosine kinase Jak1 and limits acute-phase protein expression

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Shp-2 tyrosine phosphatase functions as a negative regulator of the interferon-stimulated Jak/STAT pathway

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Dual signaling role of the protein tyrosine phosphatase SHP-2 in regulating expression of acute-phase plasma proteins by interleukin-6 cytokine receptors in hepatic cells.

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Protein tyrosine phosphatase epsilonC selectively inhibits interleukin-6- and interleukin- 10-induced JAK-STAT signaling

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TYK2 and JAK2 are substrates of protein-tyrosine phosphatase 1B

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Protein tyrosine phosphatase 1B interacts with the activated insulin receptor

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Protein-tyrosine phosphatase 1B complexes with the insulin receptor in vivo and is tyrosine-phosphorylated in the presence of insulin

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Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene

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Identifiers

10.1016/S0006-291X(02)02291-X

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Consolidated OpenCitations Corpus – April 2017

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OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

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PubMed publication ID

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Consolidated OpenCitations Corpus – April 2017

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