{"type": "FeatureCollection", "features": [{"id": "10.1017/qpb.2025.4", "type": "Feature", "geometry": null, "properties": {"updated": "2026-09-21T16:16:29Z", "type": "Journal Article", "created": "2025-04-02", "title": "Changing paradigms for the micronutrient zinc, a known protein cofactor, as a signal relaying also cellular redox state", "description": "Abstract

The micronutrient zinc (Zn) is often poorly available but toxic when present in excess, so a tightly controlled Zn homoeostasis network operates in all organisms. This review summarizes our present understanding of plant Zn homoeostasis. In Arabidopsis, about 1,900 Zn-binding metalloproteins require Zn as a cofactor. Abundant Zn metalloproteins reside in plastids, mitochondria and peroxisomes, emphasizing the need to address how Zn reaches these proteins. Apo\uffe2\uff80\uff93Zn metalloproteins do not acquire Zn2+ from a cytosolic pool of free cations, but instead through associative ligand exchange from Zn-buffering molecules. The importance of cytosolic thiols in Zn buffering suggests that, besides elevated Zn influx, a more oxidized redox state is also predicted to cause elevated labile-bound Zn levels, consistent with the suppression of a Zn deficiency marker under oxidative stress. Therefore, we consider a broadened physiological scope in plants for a possible signalling role of Zn2+, experimentally supported only in animals to date. The micronutrient zinc (Zn) is often poorly available but toxic when present in excess, so a tightly controlled Zn homoeostasis network operates in all organisms. This review summarizes our present understanding of plant Zn homoeostasis. In Arabidopsis , about 1,900 Zn-binding metalloproteins require Zn as a cofactor. Abundant Zn metalloproteins reside in plastids, mitochondria and peroxisomes, emphasizing the need to address how Zn reaches these proteins. Apo\uffe2\uff80\uff93Zn metalloproteins do not acquire Zn 2+ from a cytosolic pool of free cations, but instead through associative ligand exchange from Zn-buffering molecules. The importance of cytosolic thiols in Zn buffering suggests that, besides elevated Zn influx, a more oxidized redox state is also predicted to cause elevated labile-bound Zn levels, consistent with the suppression of a Zn deficiency marker under oxidative stress. Therefore, we consider a broadened physiological scope in plants for a possible signalling role of Zn 2+ , experimentally supported only in animals to date.