Serine/threonine-protein kinase, GCN2-like
InterPro Protein Domain record
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description
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<p>Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [<cite idref="PUB00005115"/>]:</p><p> <ul> <li>Serine/threonine-protein kinases</li><li>Tyrosine-protein kinases</li><li>Dual specific protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)</li> </ul> </p><p>Protein kinase function has been evolutionarily conserved from <taxon tax_id="562">Escherichia coli</taxon> to human [<cite idref="PUB00020114"/>]. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation [<cite idref="PUB00015362"/>]. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [<cite idref="PUB00034898"/>], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [<cite idref="PUB00034899"/>].</p><p>This entry represents a group of Gcn2 homolgues which, like gCN2, are protein kinases that control protein translation, and therefore gene expression, by phosphorylating eukaryotic initiation factor 2 (eIF2) during amino acid starvation [<cite idref="PUB00035225"/>]. Phosphorylation of the alpha subunit of eIF2 in response to cellular stress blocks initiation of protein synthesis. When phosphorylated, eIF2 is unable to exchange GDP for GTP, a recycling event that is essential for producing the active form of eIF2 which binds and delivers the initiator Met-tRNA<sub>i</sub>Met to the translation machinery. Phosphorylation of eIF2 alpha is carried out by eIF2 alpha kinases; Gcn2 is such a kinase and is a central player in the eIF2-mediated inhibition of translation initiation [<cite idref="PUB00035226"/>].</p>
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Serine/threonine-protein kinase, GCN2-like
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