peptidyl-threonine dephosphorylation

Definition

Target type: biologicalprocess

The removal of phosphoric residues from peptidyl-O-phospho-L-threonine to form peptidyl-threonine. [GOC:bf]

Peptidyl-threonine dephosphorylation is the removal of a phosphate group from a threonine residue within a protein. This process is catalyzed by a specific type of protein phosphatase known as a threonine-specific protein phosphatase. The phosphate group is typically attached to the hydroxyl group of the threonine side chain, forming a phosphothreonine residue. This phosphorylation event can alter the protein's conformation, activity, localization, or interactions with other proteins. Dephosphorylation reverses this modification, restoring the protein to its original state. The process begins when the protein phosphatase binds to the phosphorylated threonine residue. The enzyme then utilizes a nucleophilic attack by a water molecule, facilitated by the enzyme's active site residues, to break the phosphodiester bond between the phosphate group and the threonine. The phosphate group is released as inorganic phosphate (Pi) and the threonine residue is dephosphorylated. This dephosphorylation event can have significant regulatory effects on various cellular processes. For instance, it can activate or inactivate enzymes, regulate protein-protein interactions, control the localization of proteins, and influence cell signaling pathways. The precise role of peptidyl-threonine dephosphorylation depends on the specific protein and the context in which it occurs. Understanding the intricacies of this process is crucial for unraveling the complexity of cellular regulation and for developing therapeutic strategies targeting protein phosphorylation.'
"

Proteins (6)

Compounds (9)