Sandbox Reserved 427: Difference between revisions

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Interactions with insulin (IRS-1) and subsequent binding/phosphorylation. This leads to an increase in the glucose transporter (Glut-4) which has a high affinity for glucose molecules. This occurs mainly in muscle and adipose tissues where glucose uptake is most needed. This increase in Glut-4 causes an increase in glucose uptake from blood. Simply stated, 3loh is activated by insulin which signals for an increase in Glut-4. Glut-4 finds its way to the cell surface where it can perform its function (transport glucose into the cell).
The insulin receptor's main substrate is insulin, which is referred to as insulin receptor substrate 1 (IRS-1). Upon binding to IRS-1, the insulin receptor phosphorylates at least 3 tyrosine residues in IRS-1. These tyrosines are known to be located at residues 1158, 1162, and 1163. Phosphorylation of these 3 tyrosines, and possibly more, leads to an increase in the glucose transporter (Glut-4) which has a high affinity for glucose molecules. This occurs mainly in muscle and adipose tissues where glucose uptake is most needed. This increase in Glut-4 causes an increase in glucose uptake from blood. Simply stated, 3loh is activated by insulin (IRS-1) which signals for an increase in Glut-4. Glut-4 finds its way to the cell surface where it can perform its function (transport glucose into the cell).


Green scene of the active site of 3loh (tyrosine kinase) <scene name='Sandbox_Reserved_427/Active_site/1'>Active Site</scene>. This green scene is quite complex! Simplify to make your point clearly... Prof T.
Green scene of the active site of 3loh (tyrosine kinase) <scene name='Sandbox_Reserved_427/Active_site/1'>Active Site</scene>. This green scene is quite complex! Simplify to make your point clearly... Prof T.