Abstract：
:We have located the distal boundary of the tyrosine kinase domain of the EGF receptor and have identified a distinct sequence in the C' terminus required for EGF-dependent receptor internalization, leading to receptor down-regulation and degradation. Within this receptor domain, an 18 amino acid highly negatively charged region of predicted helical structure is required both for endocytosis via a high-affinity, saturable pathway and for ligand-stimulated increases in cytosolic calcium. In contrast to kinase-inactive, internalization-competent receptors, kinase-active, internalization-defective receptors effectively signaled gene transcription, morphological transformation, and growth. These observations support the hypothesis that mitogenic responses to EGF are mediated by activation of the intrinsic protein tyrosine kinase activity of the membrane-bound receptor, with ligand-induced internalization serving to terminate the signal.
journal_name
Celljournal_title
Cellauthors
Chen WS,Lazar CS,Lund KA,Welsh JB,Chang CP,Walton GM,Der CJ,Wiley HS,Gill GN,Rosenfeld MGdoi
10.1016/0092-8674(89)90867-2subject
Has Abstractpub_date
1989-10-06 00:00:00pages
33-43issue
1eissn
0092-8674issn
1097-4172pii
0092-8674(89)90867-2journal_volume
59pub_type
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