What happens when serine is phosphorylated?

What happens when serine is phosphorylated?

Phosphorylation on amino acids, such as serine, threonine, and tyrosine results in the formation of a phosphoprotein, when the phosphate group of the phosphoprotein reacts with the -OH group of a Ser, Thr, or Tyr sidechain in an esterification reaction.

How do you detect phosphorylation?

Methods for Detecting Protein Phosphorylation

  1. Introduction.
  2. Kinase Activity Assays.
  3. Phospho-Specific Antibody Development.
  4. Western Blot.
  5. Enzyme-Linked Immunosorbent Assay (ELISA)
  6. Cell-Based ELISA.
  7. Intracellular Flow Cytometry and ICC/IHC.
  8. Mass Spectrometry.

How does phosphorylation affect serine?

Diagram of serine phosphorylation. Enzyme-catalyzed proton transfer from the (–OH) group on serine stimulates the nucleophilic attack of the γ-phosphate group on ATP, resulting in transfer of the phosphate group to serine to form phosphoserine and ADP.

Can serine residues be phosphorylated?

Abstract. Phosphorylation of proteins on serine, threonine, and tyrosine residues is a major mechanism for regulating the activity of cell proteins and it plays a central role in virtually all signal transduction pathways in eukaryotes.

Why can serine be phosphorylated?

Probably because adding a phosphate group can change the conformation of a protein in a big way. Phosphorylations are usually on serines or threonines (sometime tyrosines), which are slightly polar, but almost neutral amino acids. When a phosphate is added to this, the amino acid becomes extremely polar.

How does a phosphorylation cascade work?

A phosphorylation cascade is a sequence of signaling pathway events where one enzyme phosphorylates another, causing a chain reaction leading to the phosphorylation of thousands of proteins. This can be seen in signal transduction of hormone messages.

What two enzymes control the phosphorylation of proteins and what reaction do they catalyze?

Protein phosphorylation is catalyzed by enzymes known as protein kinases, while the reverse reaction (i.e., removal of phosphates from proteins) is mediated by protein phosphatases (Manning, Whyte, Martinez, Hunter, & Sudarsanam, 2002).

How does Western blot detect phosphorylation?

To detect a low abundance protein that is weakly phosphorylated, use antibody to immunoprecipitate the protein in order to concentrate and load more protein in the sample lane. Use highly sensitive substrates for chemiluminescence detection .

How does phosphorylation increase the reactivity of glucose?

Phosphorylation allows cells to accumulate sugars because the phosphate group prevents the molecules from diffusing back across their transporter. Phosphorylation of glucose is a key reaction in sugar metabolism because many sugars are first converted to glucose before they are metabolized further.

How is protein phosphorylation regulated?

Protein kinases and phosphatases are regulated by protein-protein interactions, binding of ligands, and reversible or irreversible covalent modifications such as phosphorylation and limited proteolysis.