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Article

A domain in the transcription activator Gln3 specifically required for rapamycin responsiveness.

The Journal of biological chemistry - 4 Jul 2014

Rai Rajendra, Tate Jennifer J, Shanmuganatham Karthik, Howe Martha M, Cooper Terrance G

Abstract excerpt

Nitrogen-responsive control of Gln3 localization is implemented through TorC1-dependent (rapamycin-responsive) and TorC1-independent (nitrogen catabolite repression-sensitive and methionine sulfoximine (Msx)-responsive) regulatory pathways. We previously demonstrated amino acid substitutions in a putative Gln3 α-helix(656-666), which are required for a two-hybrid Gln3-Tor1 interaction, also abolished rapamycin...

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Identifiers

PMID: 24847055
DOI: 10.1074/jbc.M114.563668
PMCID: PMC4081939

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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.

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A domain in the transcription activator Gln3 specifically required for rapamycin responsiveness.PMID 24847055Read ↗

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