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9. What happens when a trimeric G a. Ga separates from b. GB separates from the GaG protein is activated by the GpGy dimer di
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9)G α subunit separated from GβG γ dimer

G proteins have large extracellular binding domain when a appropriate protein binds to this domain the receptor undergoes a conformation change that is transmitted to its cytosolic region which activate trimeric GTP binding protein composed of alpha, beta and gamma both alpha and gamma are covalently attached to lipid and alpha subunit has GDP bound to it when a signal received the GDP is converted to GTP and the alpha subunit gets separated form beta and gamma complex.

10) Phosphorylation of kinases such as BARK or rhodopsin kinase leading to arrestin binding.

For the switch off of GPCR it down regulation is important for the that one of the mechanism is that the kinases phosphorylate the membrane associated G proteins as the phosphate block the docking site at the G proteins by which the trimeric GPCR proteins cannot bind to the GPCR receptor site thus how it is down regulated.

11) Dephosphorylation of SHP1

    Cytokine receptor consist of tow chains each having extra cellular space for binding of cytokines, in the presence of cytokine the two chains attach by to its site able to phosphorylate the tails of cytokine receptors which will attract the signal transduction hence will get phosphorylate and enters the cells for transcription and if the cytokine receptor are dephosphorylated then it can be down regulated.

12) Endoctyosis followed by degradation by lysosomes

The cytokines receptors attracts the MHC complex which present the defected cells to t cells leading to endoctyosis and degradation by lysosomes

13) Endoctyosis followed by degradation by lysosomes

Tyrosine kinase receptor attracts the proteins which will cause the endoctyosis and degradation of cells

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