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The regulation of PP1: How to change its activity through different regulatory subunits?
Protein phosphatase 1 (PP1) is an enzyme called protein serine/threonine phosphatase, which includes metal-dependent protein phosphatases (PPMs) and aspartic acid-based Phosphatase.PP1 plays an important role in glycogen metabolism, muscle contraction, cellular process, neural activity, RNA splicing, mitosis, cell division, apoptosis, protein synthesis, and regulation of membrane receptors and channels.
Structure
Each PP1 enzyme contains one catalytic subunit and at least one regulatory subunit.The catalytic subunit consists of a single domain protein of about 30 kDaltons and can form complexes with other regulatory subunits.This catalytic subunit is highly conserved in all eukaryotes, suggesting that they share a common catalytic mechanism.Catalytic subunits can also form complexes with various regulatory subunits, which play an important role in substrate specificity and intracellular localization.
The existence of regulatory subunits not only alters the activity of PP1, but also helps it perform various functions in different cellular environments.
Catalytic Mechanism
PP1's catalytic mechanism involves the binding of two metal ions, which activates water, which in turn triggers a nucleophilic attack on phosphorus atoms.This process is key to understanding PP1's function in cells.
Exogenous Inhibitor
Potential inhibitors of PP1 include a range of natural toxins such as okadaic acid and microcystin.These toxins affect the catalytic activity of PP1, thereby regulating its biological function.
Bio functions and regulation
PP1 plays a key role in regulating liver blood sugar levels and glycogen metabolism.It ensures that the opposite regulation of glycogen breakdown and synthesis is interacting.Key regulators include glycogen phosphorylase a, which acts as a sensor for sugar in hepatocytes, which in turn affects the activity of PP1.When blood sugar levels decrease, the active type state of glycogen phosphatase a strongly binds to PP1, thereby inhibiting its phosphatase activity.Conversely, when blood sugar is too high, PP1 is released, leading to activation of glycogen synthesis.
When the body's muscle signals require the decomposition of glycogen and increase blood sugar, PP1 will be adjusted as needed.
Clinical Relevance
In clinical studies, PP1 has been found to be associated with pathological mechanisms of a variety of diseases, such as Alzheimer's disease and AIDS.Studies have shown that PP1 activity is significantly reduced in the brain of patients with Alzheimer's disease, indicating its potential role in disease development.
Subunit composition
PP1 is a multisubunit enzyme that may contain the following subunits: catalytic subunits PPP1CA, PPP1CB, PPP1CC, and a series of regulatory subunits.
Through these different regulatory subunits, the activity of PP1 can be finely regulated, making its functions more diverse in organisms.Can such regulation effectively respond to various metabolic, neurological and other physiological needs, and to what extent can it affect the development of the disease?
