(Q28144113)

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Serine phosphorylation and maximal activation of STAT3 during CNTF signaling is mediated by the rapamycin target mTOR

scientific article (publication date: 13 January 2000)

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Serine phosphorylation and maximal activation of STAT3 during CNTF signaling is mediated by the rapamycin target mTOR (English)

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K Yokogami

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S Wakisaka

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2

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J Avruch

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3

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S A Reeves

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language of work or name

English

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publication date

13 January 2000

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published in

Current Biology

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volume

10

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page(s)

47-50

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1

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Interleukin-6-type cytokine signalling through the gp130/Jak/STAT pathway

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Coordinate regulation of STAT signaling and c-fos expression by the tyrosine phosphatase SHP-2.

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Activation of phosphatidylinositol 3-kinase through glycoprotein 130 induces protein kinase B and p70 S6 kinase phosphorylation in cardiac myocytes

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Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation

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STAT3 serine phosphorylation by ERK-dependent and -independent pathways negatively modulates its tyrosine phosphorylation

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STAT3 is a serine kinase target in T lymphocytes. Interleukin 2 and T cell antigen receptor signals converge upon serine 727.

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Rapid inhibition of interleukin-6 signaling and Stat3 activation mediated by mitogen-activated protein kinases

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STATs and MAPKs: obligate or opportunistic partners in signaling

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The TOR signalling pathway and growth control in yeast

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Control of p70 s6 kinase by kinase activity of FRAP in vivo

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Integration of Jak-Stat and AP-1 signaling pathways at the vasoactive intestinal peptide cytokine response element regulates ciliary neurotrophic factor-dependent transcription

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Regulation of eIF-4E BP1 phosphorylation by mTOR.

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The mammalian target of rapamycin phosphorylates sites having a (Ser/Thr)-Pro motif and is activated by antibodies to a region near its COOH terminus

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Comparison of the specificities of p70 S6 kinase and MAPKAP kinase-1 identifies a relatively specific substrate for p70 S6 kinase: the N-terminal kinase domain of MAPKAP kinase-1 is essential for peptide phosphorylation

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7 January 2021

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inferred from DOI database lookup

1 reference

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Crossref

reference URL

https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2900268-7

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7 January 2021

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Inhibition of protein phosphatase 2A induces serine/threonine phosphorylation, subcellular redistribution, and functional inhibition of STAT3.

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7 January 2021

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Regulation of protein phosphatase 2A catalytic activity by alpha4 protein and its yeast homolog Tap42

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7 January 2021

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Protein phosphatase 2A interacts with the 70-kDa S6 kinase and is activated by inhibition of FKBP12-rapamycinassociated protein

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7 January 2021

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Phosphorylation of the translational repressor PHAS-I by the mammalian target of rapamycin

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7 January 2021

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Identifiers

DOI

10.1016/S0960-9822(99)00268-7

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1632878

OpenCitations bibliographic resource ID

1632878

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1632878

(Q28144113)

Serine phosphorylation and maximal activation of STAT3 during CNTF signaling is mediated by the rapamycin target mTOR

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