Editing Tyrosine kinase (section)

===Other examples===
Additional instances of factor-influenced protein tyrosine kinase activity, similar to this one, exist. An adapter protein such as [[Grb2]] will bind to phosphate-tyrosine residues under the influence of receptor protein kinases. This mechanism is an ordinary one that provokes protein-protein interactions.<ref name="Lehninger_2008"/>

Furthermore, to illustrate an extra circumstance, insulin-associated factors have been determined to influence tyrosine kinase. [[Insulin receptor substrate]]s are molecules that function in signaling by regulating the effects of insulin.<ref name="Lehninger_2008"/> Many receptor enzymes have closely related structure and receptor tyrosine kinase activity, and it has been determined that the foundational or prototypical receptor enzyme is insulin.<ref name="Lehninger_2008"/> Insulin receptor substrates [[IRS2]] and [[IRS3]] each have unique characteristic tissue function and distribution that serves to enhance signaling capabilities in pathways that are initiated by receptor tyrosine kinases.<ref name="Lehninger_2008"/> Activated [[IRS-1]] molecules ''enhance'' the signal created by insulin.<ref name="Lehninger_2008"/> The insulin receptor system, in contrast, appears to ''diminish'' the efficacy of endosomal signaling.<ref name="Wiley_2001"/>

The [[epidermal growth factor receptor]] system, as such, has been used as an intermediate example.<ref name="Wiley_2001"/> Some signals are produced from the actual cell surface in this case but other signals seem to emanate from within the [[endosome]]s. This variety of function may be a means to create ligand-specific signals.<ref name="Wiley_2001"/> This supports the notion that trafficking, a term for the modification of proteins subsequent to mRNA translation, may be vital to the function of receptor signaling.

<gallery>
Image:L-tyrosine-skeletal.png|[[Tyrosine]]
Image:Phosphate Group.svg|[[Phosphate]]
Image:ATP structure revised.svg|[[Adenosine triphosphate|ATP]]
</gallery>