dephosphorylerer

Dephosphorylering, or dephosphorylation, is the enzymatic removal of phosphate groups from substrates, most commonly proteins but also lipids and nucleotides. The reaction is catalyzed by phosphatases and results in the formation of inorganic phosphate. In Norwegian, dephosphorylerer is the present tense verb meaning “dephosphorylates,” while dephosphorylering refers to the process itself.

Protein phosphatases are categorized by substrate preference: serine/threonine phosphatases remove phosphate from serine or threonine residues; tyrosine phosphatases target tyrosine residues; and dual-specificity phosphatases can act on more than one type of residue. Most phosphatases operate through hydrolytic mechanisms that often require metal ions and produce inorganic phosphate as a product.

Dephosphorylation is a counterbalance to phosphorylation, the addition of phosphate groups by kinases. The dynamic cycle of phosphorylation and dephosphorylation modulates protein activity, interactions, localization, and stability, thereby regulating signaling pathways, cell division, metabolism, and responses in neurons and immune cells.

Prominent phosphatases include PP1, PP2A, and calcineurin (PP2B) for serine/threonine substrates, and various protein tyrosine phosphatases for tyrosine substrates; lipid phosphatases such as PTEN also influence signaling. Dysregulation of dephosphorylation is linked to diseases including cancer, diabetes, and neurodegeneration. Pharmacological modulation of phosphatases is an active area of research, with therapeutic agents such as calcineurin inhibitors used in transplantation and autoimmune diseases.