Protein phosphorylation

Protein phosphorylation is the covalent addition of a phosphate group to a protein, usually on serine, threonine, or tyrosine. It can alter the protein’s activity, location, stability, or interactions.

Protein kinase: An enzyme that transfers a phosphate group, usually from ATP, to a protein substrate. Kinases catalyze the phosphate addition that defines this modification.
MAPK/ERK pathway: A signaling cascade that relays extracellular cues through mitogen-activated protein kinases to cellular responses. Sequential phosphorylation carries signals through this widely studied pathway.
Serine: A proteinogenic amino acid with a hydroxyl-bearing side chain. Its hydroxyl group is a common target for protein phosphorylation.
Protein acetylation: The covalent addition of an acetyl group to a protein, often on lysine residues or at the N-terminus. Acetylation modifies proteins with a different chemical group and distinct regulatory consequences.
Signal transduction: The process by which cells convert signals into molecular and cellular responses. Phosphorylation is a common molecular step for relaying cellular signals.
Protein phosphatase: An enzyme that removes phosphate groups from proteins. Phosphatases reverse phosphorylation and help control its duration.
Insulin signaling pathway: A network of cellular reactions triggered when insulin binds its receptor. Receptor and downstream protein phosphorylation transmit insulin’s metabolic signal.
Threonine: A proteinogenic amino acid with a hydroxyl-bearing side chain and a methyl group. Its hydroxyl group can accept a phosphate in regulated proteins.
Protein ubiquitination: The attachment of ubiquitin to a protein, commonly affecting its degradation, location, or interactions. Ubiquitination uses a protein tag rather than a small phosphate group.
Allosteric regulation: Regulation of a protein’s activity through a molecule binding at a site distinct from its active site. A phosphate can reshape protein structure and alter activity at a distance.

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