Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Immunopurified mammalian target of rapamycin phosphorylates and activates p70 S6 kinase alpha in vitro.

The Journal of biological chemistry - 26 Nov 1999

Isotani S, Hara K, Tokunaga C, Inoue H, Avruch J, Yonezawa K

Abstract excerpt

p70 S6 kinase alpha (p70alpha) is activated in vivo through a multisite phosphorylation in response to mitogens if a sufficient supply of amino acids is available or to high concentrations of amino acids per se. The immunosuppressant drug rapamycin inhibits p70alpha activation in a manner that can be overcome by coexpression of p70alpha with a rapamycin-resistant mutant of the mammalian target of rapamycin (mTOR)...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to 3-Phosphoinositide-Dependent Protein Kinases
Share to Culture Media, Serum-Free

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mitogens

Share to Phosphotransferases (Alcohol Group Acceptor)

Share to Precipitin Tests

Share to Protein Kinases

Share to Ribosomal Protein S6 Kinases

Share to TOR Serine-Threonine Kinases

Source

Identifiers

PMID: 10567431
DOI: 10.1074/jbc.274.48.34493

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Immunopurified mammalian target of rapamycin phosphorylates and activates p70 S6 kinase alpha in vitro.PMID 10567431Read ↗

Identification of S6 kinase 1 as a novel mammalian target of rapamycin (mTOR)-phosphorylating kinase.Semantic proximity Read ↗

The mammalian target of rapamycin signaling pathway: twists and turns in the road to cancer therapy.Semantic proximity Read ↗

A new role for the p85-phosphatidylinositol 3-kinase regulatory subunit linking FRAP to p70 S6 kinase activation.Semantic proximity Read ↗

mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events.Semantic proximity Read ↗

The influence of mTOR inhibitors on immunity and the relationship to post-transplant malignancySemantic proximity Read ↗

The rapamycin-binding domain governs substrate selectivity by the mammalian target of rapamycin.Semantic proximity Read ↗

The Src-family tyrosine kinase inhibitor PP1 interferes with the activation of ribosomal protein S6 kinases.Semantic proximity Read ↗

The insulin-induced signalling pathway leading to S6 and initiation factor 4E binding protein 1 phosphorylation bifurcates at a rapamycin-sensitive point immediately upstream of p70s6k.Semantic proximity Read ↗

mTORC1-S6K activation by endotoxin contributes to cytokine up-regulation and early lethality in animals.Semantic proximity Read ↗

Differential effects of rapamycin on mammalian target of rapamycin signaling functions in mammalian cells.Semantic proximity Read ↗

Mechanistic target of rapamycin complex 1 (mTORC1)-mediated phosphorylation is governed by competition between substrates for interaction with raptor.Semantic proximity Read ↗

mTOR regulates skeletal muscle regeneration in vivo through kinase-dependent and kinase-independent mechanisms.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.