Sandbox Reserved 1627: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 41: | Line 41: | ||
===At the Cellular Level=== | ===At the Cellular Level=== | ||
The conformation change from the inactive to active state upon insulin binding has a time constant of six minutes. Autophosphorylation of the beta subunits reaches a maximal level in about one minute, and lasts for approximately six to ten minutes. One insulin receptor substrate has a half-life of 3.5 minutes where it is able to be phosphorylated by the tyrosine kinases of the beta subunit and then act as a central hub for further downstream signaling pathways. Once insulin binds to the alpha subunit, the receptor remains active for approximately ten minutes before the insulin is degraded and the receptor returns to its inactive conformation. This time frame puts a perspective on how long it takes for the human body to store excess glucose in their blood stream from a recent meal as glycogen for later use as fuel. <ref name="Tatulian" /> | The conformation change from the inactive to active state upon insulin binding has a [http://en.wikipedia.org/wiki/Time_constant time constant] of six minutes. Autophosphorylation of the beta subunits reaches a maximal level in about one minute, and lasts for approximately six to ten minutes. One insulin receptor substrate has a half-life of 3.5 minutes where it is able to be phosphorylated by the tyrosine kinases of the beta subunit and then act as a central hub for further downstream signaling pathways. Once insulin binds to the alpha subunit, the receptor remains active for approximately ten minutes before the insulin is degraded and the receptor returns to its inactive conformation. This time frame puts a perspective on how long it takes for the human body to store excess glucose in their blood stream from a recent meal as glycogen for later use as fuel. <ref name="Tatulian" /> | ||
