Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Cell. 1995 Jan 13;80(1):103-13.

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

Author information

  • 1Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.

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.

PMID:
7529140
[PubMed - indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk