peptidyl-serine dephosphorylation

Definition

Target type: biologicalprocess

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

Peptidyl-serine dephosphorylation is a crucial biological process that involves the removal of a phosphate group from a serine residue within a protein. This process is catalyzed by a specific class of enzymes known as protein phosphatases. These phosphatases recognize and bind to the phosphorylated serine residue, facilitating the hydrolysis of the phosphate group, releasing inorganic phosphate (Pi) and restoring the dephosphorylated serine residue.

Peptidyl-serine dephosphorylation plays a vital role in regulating a wide range of cellular processes, including signal transduction, cell growth, differentiation, and metabolism. By removing phosphate groups from target proteins, phosphatases can effectively switch off signaling pathways, modulate protein activity, and alter protein-protein interactions.

The mechanism of peptidyl-serine dephosphorylation involves several key steps:

1. **Substrate recognition and binding:** The phosphatase enzyme recognizes and binds to the phosphorylated serine residue on the target protein. This recognition often involves specific amino acid sequences or structural motifs surrounding the phosphorylation site.
2. **Catalysis:** Once bound, the phosphatase catalyzes the hydrolysis of the phosphate group. This process typically involves the formation of a transient covalent intermediate between the phosphatase and the phosphate group.
3. **Phosphate release:** The hydrolyzed phosphate group is released from the protein as inorganic phosphate (Pi).
4. **Dephosphorylated protein:** The target protein is now dephosphorylated and its activity or conformation may be altered.

Peptidyl-serine dephosphorylation is highly regulated and can be influenced by factors such as:

* **Phosphatase activity:** The activity of phosphatases can be regulated by various mechanisms, including phosphorylation, protein-protein interactions, and cellular localization.
* **Substrate availability:** The availability of phosphorylated substrates can also influence the rate of dephosphorylation.
* **Cellular environment:** The cellular environment, including pH, ion concentrations, and the presence of other molecules, can also affect phosphatase activity.

Overall, peptidyl-serine dephosphorylation is a fundamental biological process that plays a critical role in maintaining cellular homeostasis and regulating a wide range of cellular functions. Understanding the intricacies of this process is essential for comprehending the complexity of cellular signaling and the mechanisms underlying various physiological processes.'
"

Proteins (3)

Compounds (5)