protein serine/threonine phosphatase complex

Definition

Target type: cellularcomponent

A complex, normally consisting of a catalytic and a regulatory subunit, which catalyzes the removal of a phosphate group from a serine or threonine residue of a protein. [GOC:bf]

Protein serine/threonine phosphatase complexes are intricate assemblies of proteins that play a critical role in cellular signaling and regulation. These complexes often comprise a catalytic subunit, which possesses the enzymatic activity to dephosphorylate serine and threonine residues on target proteins. The catalytic subunit is typically associated with one or more regulatory subunits that modulate its activity and substrate specificity. Regulatory subunits can include scaffolding proteins that provide structural support and promote the assembly of the complex, as well as targeting subunits that direct the complex to specific cellular locations or substrates. The cellular component of protein serine/threonine phosphatase complexes can vary depending on the specific complex and its function. Some complexes reside in the cytoplasm, where they regulate intracellular signaling pathways, while others associate with membranes, where they modulate the activity of membrane-bound proteins. Additionally, some complexes are localized to the nucleus, where they regulate gene expression and other nuclear processes. The localization and composition of protein serine/threonine phosphatase complexes are tightly regulated, allowing for precise control of their activity in different cellular compartments. This intricate regulation ensures that these complexes can effectively respond to diverse cellular stimuli and maintain cellular homeostasis.'
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Proteins (4)

Compounds (5)