Sandbox Reserved 1490: Difference between revisions
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===• Signal transduction and kinase activity=== | ===• Signal transduction and kinase activity=== | ||
Receptor tyrosine kinases are transmembrane proteins with a | Receptor tyrosine kinases are transmembrane proteins with a [[2gy5|ligand-binding extracellular domain]], a single membrane-spanning domain, a juxtamembrane region, a catalytic domain, and a C-terminal tail.<ref>PMID:11513602</ref> In cell culture, ANGPT1 induces phosphorylation of TIE2 and stimulates endothelial cell migration and survival. | ||
The activation of the receptor is due to a ligand-induced dimerization : the extracellular receptor domain dimerization brings the cytosolic kinase domains next to each other for intermolecular autophosphorylation. The latter occurs when one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. It happens in a sequential manner : Tyr-992 in the kinase activation loop is phosphorylated first, followed by autophosphorylation at Tyr-1108 and at additional tyrosine residues. Autophosphorylation also has multiple functions including recruitment of downstream signaling molecules.<ref>PMID:11513602</ref> | The activation of the receptor is due to a ligand-induced dimerization : the extracellular receptor domain dimerization brings the cytosolic kinase domains next to each other for intermolecular autophosphorylation. The latter occurs when one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. It happens in a sequential manner : Tyr-992 in the kinase activation loop is phosphorylated first, followed by autophosphorylation at Tyr-1108 and at additional tyrosine residues. Autophosphorylation also has multiple functions including recruitment of downstream signaling molecules.<ref>PMID:11513602</ref> | ||