Identification of an intracellular domain of the EGF receptor required for high-affinity binding of EGF.
Although all EGF receptors in EGF receptor-expressing cells are molecularly identical, they can be subdivided in two different classes that have either a high or a low affinity for EGF. Specifically the high-affinity class is associated with filamentous actin. To determine whether the interaction of the EGF receptor with actin induces its high-affinity state, we studied EGF-binding properties of an EGF receptor mutant that lacks the actin-binding site. Interestingly, we found that cells expressing this mutant receptor still display both high- and low-affinity classes of EGF receptors, indicating that the actin-binding domain does not determine the high-affinity binding state. By further mutational analysis we identified a receptor domain, within the tyrosine kinase domain, that regulates the affinity for EGF.
Van der Heyden
M A
MA
Department of Molecular Cell Biology, Institute of Biomembranes, Universiteit Utrecht, The Netherlands.
Nievers
M
M
Verkleij
A J
AJ
Boonstra
J
J
Van Bergen en Henegouwen
P M
PM
D016475:3T3 Cells; D000199:Actins / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D004815:Epidermal Growth Factor / Q000378:metabolism*; D066246:ErbB Receptors / Q000235:genetics / Q000378:metabolism*; D007425:Intracellular Membranes / Q000378:metabolism; D051379:Mice; D017384:Sequence Deletion
D000199:Actins; D004815:Epidermal Growth Factor; D066246:ErbB Receptors