So in the second method we have a special protein kinase we call the beta Adrenergic receptor kinase and it's basically a kinase protein which means it uses ATP to actually add or phosphorylate that particular protein. So the beta Adrenergic receptor kinase uses ATP to actually phosphorylate the carboxyl terminal side of this protein which is found on the intracellular side. And so we essentially add these negatively charged phosphate groups onto this structure and that decreases its affinity to basically go on and activate these alphagy proteins. On top of that, we have a second type of molecule, a protein we call beta arrestin that goes on and binds to these phosphate groups and that further decreases the ability of these complexes, the epinephrine receptor complex, to actually activate those alphagy proteins. So in a second mode of inactivation, the beta Adrenergic receptor kinase basically phosphorylates the carboxylic terminal end of that ethanephone receptor complex on the intracellular side of that protein. So this protein kinase uses ATP to put asphorylated and then the beta arrestin binds onto these phosphate groups and that inactivates the receptor's ability to stimulate those alphagy proteins to basically transform the GDP into the GTP form of that alpha g protein.