Loss of an amino acid transporter and tissue depletion of nitric oxide worsens the intestinal function of CF mice, a finding that potentially explains variation in disease severity amongst CF individuals.

Activation by amino acids causes mTORC1 to translocate transiently to the lysosomal surface.

Quantitative de novo proteomics paired with in vivo cell-specific non-canonical amino acid labelling identified several spatial long-term memory-induced changes in protein synthesis in hippocampal neurons.

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

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.

The ZNRF2 enzyme helps the mTOR protein complex to sense amino acid levels and regulate mammalian cell growth.

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

Single-molecule measurement of conformational dynamics using a genetically encoded fluorescent probe suggests that the selectivity filter region of TRPV1 channels undergoes dynamic motion during agonist activation.

Enzymatic division of labor is identified as an enabling biochemical strategy for regulating a family of structurally diverse bioactive lipids.

Despite BCAAs being de novo-synthesized in chloroplasts, TOR activation by BCAAs is conserved in plants and triggers a re-organization of actin and actin-associated endomembranes.