High-Throughput Identification of Calcium Regulated Proteins Across Diverse Proteomes.

ABSTRACT: Calcium ions play important roles in nearly every biological process, yet whole-proteome analysis of calcium effectors has been hindered by lack of high-throughput, unbiased, and quantitative methods to identify proteins-calcium engagement. To address this, we adapted protein thermostability assays in the budding yeast, human cells, and mouse mitochondria. Based on calcium-dependent thermostability, we identified 2884 putative calcium-regulated proteins across human, mouse, and yeast proteomes. These data revealed calcium engagement of novel signaling hubs and cellular processes, including metabolic enzymes and the spliceosome. Cross-species comparison of calcium-protein engagement and mutagenesis experiments identified residue-specific cation engagement, even within well-known EF-hand dom

SUBMITTER: Locke TM 

PROVIDER: S-EPMC10827220 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature