Abstract:
:Receptor dimerization is ubiquitous to the action of all receptor tyrosine kinases, and in the case of dimeric ligands, such as the stem cell factor (SCF), it was attributed to ligand bivalency. However, by using a dimerization-inhibitory monoclonal antibody to the SCF receptor, we confined a putative dimerization site to the nonstandard fourth immunoglobulin-like domain of the receptor. Deletion of this domain not only abolished ligand-induced dimerization and completely inhibited signal transduction, but also provided insights into the mechanism of the coupling of ligand binding to dimer formation. These results identify an intrinsic receptor dimerization site and suggest that similar sites may exist in other receptors.
journal_name
Celljournal_title
Cellauthors
Blechman JM,Lev S,Barg J,Eisenstein M,Vaks B,Vogel Z,Givol D,Yarden Ydoi
10.1016/0092-8674(95)90455-7subject
Has Abstractpub_date
1995-01-13 00:00:00pages
103-13issue
1eissn
0092-8674issn
1097-4172pii
0092-8674(95)90455-7journal_volume
80pub_type
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