Emerging functions of cysteine synthase complexes in plants

Cysteine biosynthesis is the entry point of reduced sulfur into plant metabolism, and underlies the formation of numerous sulfur-containing compounds essential for stress adaptation. Cysteine is produced by the consecutive action of serine acetyltransferase (SERAT) and O-acetylserine-(thiol)lyase (OAS-TL), which assemble into the cysteine synthase complex (CSC). Formation of the CSC is reversible and regulated by the cysteine precursors O-acetylserine (OAS) and sulfide, linking cysteine production to the cellular status of carbon, nitrogen, and sulfur. Traditionally, the CSC has been hypothesized as a metabolic sensor of the carbon/nitrogen and sulfur supply for cysteine biosynthesis. However, recent studies reveal a broader role. The CSC is present in multiple sub-cellular compartments and shows functional diversity across plant species. Emerging evidence shows that CSC dynamics are tightly integrated with environmental signaling pathways, enabling plants to coordinate sulfur metabolism with responses to stress conditions such as high light, drought, heavy metals, and pathogen challenge. In this review, we synthesize recent advances in the characterization of SERAT and OAS-TL proteins, and highlight the CSC as a regulatory hub that integrates metabolic status with stress signaling to respond to specific environmental stimuli.