Amy Palmer

University of Colorado Boulder - US

There are over two thousand proteins encoded by the human genome that bind zinc, where zinc binding is predicted to be essential for function. At the cellular level zinc is important for DNA synthesis, cell proliferation, differentiation, and apoptosis.

Given the importance of Zn²⁺ in cell biology and human health, it is astounding that we still don’t understand the mechanisms of how Zn²⁺ levels and dynamics impact basic cellular functions and give rise to disease.

Our lab has developed a suite of genetically encoded fluorescent sensors for Zn²⁺ and has used these sensors to quantify Zn²⁺ in different organelles in mammalian cells. Our results reveal that the labile Zn²⁺ pool is very low (hundreds of pM in the cytosol) but that cells experience Zn²⁺ dynamics and fluxes in response to cellular processes and environmental perturbations. Although the conventional view of Zn²⁺ in biology is that it is constitutively and stably bound to the proteins that comprise the zinc proteome, there is growing evidence that the proteome may sense and respond to Zn²⁺ dynamics in cells.

We have discovered that Zn²⁺ dynamics profoundly influence fundamental cellular processes such as gene expression, interactions between transcription factors and chromatin, and the mammalian cell cycle.