Dephosphorylerar

Dephosphorylerar is the biochemical process by which phosphate groups are removed from molecules, most often from proteins. It is the functional opposite of phosphorylation and is a central mechanism for regulating protein activity, cellular signaling, and metabolism in living cells. By removing phosphate groups, dephosphorylerar can terminate signaling events, alter enzyme activity, modify protein interactions, and influence subcellular localization.

Enzymes that carry out dephosphorylation are called phosphatases. Major classes include protein tyrosine phosphatases (PTPs), serine/threonine phosphatases (such as PP1, PP2A, PP2B), and dual-specificity phosphatases (DUSPs) that can remove phosphates from multiple amino acid residues. In addition, lipid and sugar dephosphorylation is performed by lipid phosphatases like PTEN and various inorganic and organic phosphatases acting on small molecules. The activity of phosphatases is tightly regulated and often counterbalances kinases in signaling networks.

In cells, dephosphorylerar shapes pathways such as MAPK signaling, PI3K/AKT signaling, and cell cycle control. For example, mitogen-activated protein kinase phosphatases (MKPs) deactivate MAP kinases by removing phosphate groups, while PTEN reduces PIP3 levels to suppress AKT signaling. Dysregulation of dephosphorylation is linked to diseases including cancer, metabolic disorders, and neurodegeneration. Regulation occurs through factors like subcellular localization, inhibitor proteins, redox state, and post-translational modifications of phosphatases themselves.