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Article

Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast.

Science (New York, N.Y.) - 23 Aug 1991

Heitman J, Movva N R, Hall M N

Abstract excerpt

FK506 and rapamycin are related immunosuppressive compounds that block helper T cell activation by interfering with signal transduction. In vitro, both drugs bind and inhibit the FK506-binding protein (FKBP) proline rotamase. Saccharomyces cerevisiae cells treated with rapamycin irreversibly arrested in the G1 phase of the cell cycle. An FKBP-rapamycin complex is concluded to be the toxic agent because (i)...

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Source

Identifiers

PMID: 1715094
DOI: 10.1126/science.1715094

Genes

FPR1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast.PMID 1715094Read ↗

TOR mutations confer rapamycin resistance by preventing interaction with FKBP12-rapamycin.Semantic proximity Read ↗

Antifungal properties of the immunosuppressant FK-506: identification of an FK-506-responsive yeast gene distinct from FKB1.Semantic proximity Read ↗

Dominant missense mutations in a novel yeast protein related to mammalian phosphatidylinositol 3-kinase and VPS34 abrogate rapamycin cytotoxicity.Semantic proximity Read ↗

Rapamycin Antifungal Action Is Mediated via Conserved Complexes with FKBP12 and TOR Kinase Homologs in Cryptococcus neoformansSemantic proximity Read ↗

The fission yeast TOR homolog, tor1+, is required for the response to starvation and other stresses via a conserved serine.Semantic proximity Read ↗

Protein kinase activity and identification of a toxic effector domain of the target of rapamycin TOR proteins in yeast.Semantic proximity Read ↗

A novel FK506- and rapamycin-binding protein (FPR3 gene product) in the yeast Saccharomyces cerevisiae is a proline rotamase localized to the nucleolus.Semantic proximity Read ↗

Rapamycin exerts antifungal activity in vitro and in vivo against Mucor circinelloides via FKBP12-dependent inhibition of Tor.Semantic proximity Read ↗

Fpr1, a primary target of rapamycin, functions as a transcription factor for ribosomal protein genes cooperatively with Hmo1 in Saccharomyces cerevisiaeSemantic proximity Read ↗

The rapamycin-binding domain of the protein kinase mammalian target of rapamycin is a destabilizing domain.Semantic proximity Read ↗

Rapamycin inhibits yeast nucleotide excision repair independently of tor kinases.Semantic proximity Read ↗

Missense mutations at the FKBP12-rapamycin-binding site of TOR1.Semantic proximity Read ↗

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