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Concept
Autophosphorylation
Summary
Autophosphorylation is a type of post-translational modification of proteins. It is generally defined as the phosphorylation of the kinase by itself. In eukaryotes, this process occurs by the addition of a phosphate group to serine, threonine or tyrosine residues within protein kinases, normally to regulate the catalytic activity.
Autophosphorylation may occur when a kinases' own active site catalyzes the phosphorylation reaction (cis autophosphorylation), or when another kinase of the same type provides the active site that carries out the chemistry (trans autophosphorylation). The latter often occurs when kinase molecules dimerize. In general, the phosphate groups introduced are gamma phosphates from nucleoside triphosphates, most commonly ATP.
Protein kinases, many of which are regulated by autophosphorylation, are vital in controlling the cellular proliferation, differentiation, metabolism, migration and survival. Mutations in the genes encoding them or their potential activators or repressors can affect any number of functions within an organism.
Phosphorylation is easily reversed by phosphatases. Therefore, it is an effective method of turning 'on' and 'off' kinase activity. Because of this it is recognized as an essential process in cell signaling.
Addition of a negatively charged phosphate group brings about a change in the microenvironment that may lead to attraction or repulsion of other residues or molecules. The result may be a conformational change to expose or hide catalytic or allosteric seats from the surface.
If the phosphorylated residue resides within the catalytic seat itself, it may facilitate or prevent substrate binding by means of charge-interaction, or by providing or preventing complementary shapes necessary for molecular recognition. In addition, the phosphate group yields several potential areas for hydrogen-bonding or establishment of salt-bridges, of which the latter generally involves an arginine residue.
Binding of effector molecules may be affected in a similar manner if the phosphorylated residue makes part of the allosteric site.
Official source
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