Editing Dimerization (section)

=== Receptor tyrosine kinase ===
Much like for G protein-coupled receptors, dimerization is essential for [[receptor tyrosine kinase]]s (RTK) to perform their function in [[signal transduction]], affecting many different cellular processes.<ref name=":2">{{Cite journal |last=Hubbard |first=Stevan R |date=1999-04-01 |title=Structural analysis of receptor tyrosine kinases |journal=Progress in Biophysics and Molecular Biology |language=en |volume=71 |issue=3 |pages=343–358 |doi=10.1016/S0079-6107(98)00047-9 |pmid=10354703 |issn=0079-6107|doi-access=free }}</ref> RTKs typically exist as monomers, but undergo a [[conformational change]] upon [[Ligand (biochemistry)|ligand]] binding, allowing them to dimerize with nearby RTKs.<ref>{{Cite journal |last1=Lemmon |first1=Mark A. |last2=Schlessinger |first2=Joseph |date=2010-06-25 |title=Cell Signaling by Receptor Tyrosine Kinases |journal=Cell |language=English |volume=141 |issue=7 |pages=1117–1134 |doi=10.1016/j.cell.2010.06.011 |issn=0092-8674 |pmc=2914105 |pmid=20602996}}</ref><ref>{{Cite journal |last1=Lemmon |first1=Mark A. |last2=Schlessinger |first2=Joseph |last3=Ferguson |first3=Kathryn M. |date=2014-04-01 |title=The EGFR Family: Not So Prototypical Receptor Tyrosine Kinases |journal=Cold Spring Harbor Perspectives in Biology |language=en |volume=6 |issue=4 |pages=a020768 |doi=10.1101/cshperspect.a020768 |issn=1943-0264 |pmid=24691965|pmc=3970421 |doi-access=free }}</ref> The dimerization activates the [[cytoplasm]]ic [[kinase]] [[Protein domain|domains]] that are responsible for further [[signal transduction]].<ref name=":2" />