The nutrient-sensing GCN2 signaling pathway is required for robust circadian rhythm by recruiting the histone acetyltransferase GCN5 to establish a proper chromatin state at the circadian clock gene promoter under amino acid starvation in Neurospora.

Amino-acid starvation leads to the formation of a reversible stress assembly, the Sec body, which is a pro-survival reservoir for components of the ER exit sites.

Amino-acid induced Sec body formation is mediated by PARP16 dependent MARylation of Sec16, a component of the endoplasmic reticulum exit site.

Genetic lesions that compromise the ribosome P-stalk implicate direct signalling from the ribosome to the translation initiation factor eIF2 kinase GCN2 in the cellular response to amino acid starvation.

Using mass spectrometry to study protein composition of translating ribosomes under unstressed or stress conditions, aspartate aminotransferase 2 (Aat2) is identified as a metabolic enzyme with a moonlighting function in the yeast integrated stress-response pathway.

Metabolic cues enlist ubiquitin ligase adaptors for the selective control of cellular nutrient acquisition strategies.

The role of an amino acid-dependent tRNA modification as a nutrient sensor and regulator of metabolic homeostasis has been discovered.

Nutrient starvation activates autophagy by a novel signaling mechanism that is blocked by one of the major autophagy inhibitors.

Sea3, a presumed subunit of the GATOR2 complex in fission yeast, is required for the GATOR1 function that attenuates TORC1 in parallel with the TSC complex and Gcn2 kinase.

The budding yeast gained a novel regulator of TORC1 signaling, called Ait1, 150–200 million years ago, around the same time they lost functional Rheb and Tsc1/2.