Abstract
AbstractZinc is an indispensable micronutrient for optimal physiological function; therefore, zinc deficiency has been implicated in the pathogenesis of various human diseases. To address these deleterious conditions, our bodies have regulatory mechanisms that respond to zinc deficiency stress at the cellular level. However, the related molecular mechanisms, especially at the gene expression level, remain poorly understood. Here, we show that during zinc deficiency, the histone acetyltransferase KAT7 loses its enzymatic activity, leading to the attenuated acetylation of histone H3 at Lys14 (H3K14ac). Physiologically, this decrease in H3K14ac leads to the transcriptional upregulation ofZIP10, a plasma membrane-localized zinc transporter, thereby importing zinc from extracellular sources to maintain cellular zinc homeostasis. Our data demonstrate that cells respond to zinc deficiency stress by converting it into an epigenetic signal to drive cellular responses.
Publisher
Cold Spring Harbor Laboratory
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