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Proteins can connect with new binding partners thanks to phosphorylation, which modifies the structure of the protein.
Phosphorylation sites are created by protein kinases (also known as "writers"), frequently have an impact after being recognized by phospho-binding proteins (also known as "readers"), and are afterwards eliminated by protein phosphatases (also known as "erasers").
This writer-reader-eraser toolbox has been crucial in the evolution of new functionalities necessary for the development of multicellular organisms and enables phosphorylation events to control a wide range of regulatory activities. Typically modular in organization, the proteins that make up this system of protein kinases, phospho-binding targets, and phosphatases are made up of several globular domains and smaller peptide motifs having binding or catalytic capabilities.
Through genetic recombination, the linking of these binding and catalytic modules in novel ways, as well as the choice of certain domain combinations, have aided in the emergence of new, physiologically advantageous processes. Conversely,
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