The catalytic subunit of PP1 is highly conserved among eukaryotes, indicating a common catalytic mechanism . It consists of a 30-kD single-domain protein that can form complexes with various regulatory subunits . These regulatory subunits are essential for substrate specificity and compartmentalization, allowing PP1 to target specific cellular locations and processes .
PP1γ, in particular, is encoded by the PPP1CC gene and is expressed in mammalian cells . It has distinct localization patterns and interacts with a variety of regulatory subunits to execute its functions . The interaction of PP1γ with regulatory subunits is mediated by a conserved binding motif known as the RVxF motif .
The catalytic mechanism of PP1 involves the coordination of metal ions, such as manganese (Mn) and iron (Fe), which are essential for its activity . These metal ions bind and activate water molecules, initiating a nucleophilic attack on the phosphorus atom of the substrate . This process leads to the dephosphorylation of the substrate, thereby regulating its activity.
PP1γ is involved in various cellular processes, including:
PP1 is targeted by various naturally occurring inhibitors, such as okadaic acid and microcystin . These inhibitors interact with the catalytic subunit of PP1 and modulate its activity. Understanding the mode of action of PP1 and its inhibitors can facilitate the development of drugs that target specific PP1 complexes, thereby modulating the phosphorylation state of a limited subset of proteins .
In summary, Protein Phosphatase 1, Catalytic Subunit Gamma (Human Recombinant) is a critical enzyme involved in regulating numerous cellular processes. Its interaction with regulatory subunits and its catalytic mechanism make it a key player in cellular signaling pathways.