Receptor signaling: when dimerization is not enough.
Activation of receptors that signal via tyrosine kinase domains has been thought to involve receptor dimerization and transphosphorylation of juxtaposed catalytic domains. Recent results suggest things might be more complex - specific intersubunit conformational changes within a dimer can also be important.
Jiang
G
G
Molecular Biology and Virology Laboratory, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, California 92037, USA.
Hunter
T
T
D000818:Animals; D019281:Dimerization; D008958:Models, Molecular; D010766:Phosphorylation; D011487:Protein Conformation; D020836:Protein Structure, Quaternary; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000378:metabolism*; D017467:Receptors, Erythropoietin / Q000737:chemistry / Q000378:metabolism; D015398:Signal Transduction
D011956:Receptors, Cell Surface; D017467:Receptors, Erythropoietin