Fosfotomics

Fosfotomics is a subfield of phosphoproteomics that focuses specifically on the study of phosphorylated proteins within a biological system. Phosphorylation is a crucial post-translational modification where a phosphate group is added to a protein, often acting as a molecular switch that alters the protein's activity, localization, or interaction with other molecules. Fosfotomics aims to systematically identify and quantify these phosphorylated sites on proteins and to understand their functional consequences.

The techniques employed in fosfotomics are typically advanced mass spectrometry-based methods. These methods allow for the identification of thousands of phosphorylation sites across the proteome. Sample preparation often involves enrichment strategies to isolate phosphorylated peptides from the vast number of non-phosphorylated peptides. These enrichment techniques can include immobilized metal affinity chromatography (IMAC) or antibody-based methods targeting phosphoserine, phosphothreonine, or phosphotyrosine residues.

By mapping these phosphorylation events, researchers can gain insights into cellular signaling pathways, such as those involved in cell growth, differentiation, metabolism, and stress responses. Changes in phosphorylation patterns can be indicative of disease states or responses to environmental stimuli. Therefore, fosfotomics plays a vital role in understanding cellular regulation and in the discovery of potential biomarkers and therapeutic targets.