The fourth immunoglobulin domain of the stem cell factor receptor couples ligand binding to signal transduction.

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

Cell

journal_title

Cell

authors

Blechman JM,Lev S,Barg J,Eisenstein M,Vaks B,Vogel Z,Givol D,Yarden Y

doi

10.1016/0092-8674(95)90455-7

subject

Has Abstract

pub_date

1995-01-13 00:00:00

pages

103-13

issue

1

eissn

0092-8674

issn

1097-4172

pii

0092-8674(95)90455-7

journal_volume

80

pub_type

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