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Identification of an intracellular domain of the EGF receptor required for high‐affinity binding of EGF
Author(s) -
Van der Heyden Marcel A.G,
Nievers Mirjam,
Verkleij Arie J,
Boonstra Johannes,
Van Bergen en Henegouwen Paul M.P
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00599-1
Subject(s) - epidermal growth factor , receptor , microbiology and biotechnology , biology , tyrosine kinase , mutant , receptor tyrosine kinase , binding domain , egf like domain , biochemistry , chemistry , binding site , gene
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.