Development of Strategies to Manipulate ErbB Receptor Heterodimerization from a Quantitative Analysis of Receptor/Ligand Relationships
Abstract
The four erbB receptor tyrosine kinases are activated by dimerization upon binding their cognate ligands, which include epidermal growth factor (EGF) and the neuregulins (NRG's). Each receptor has a large extracellular ligand-binding domain, a single transmembrane domain, and an intracellular tyrosine kinase/regulatory domain. More than 12 different erbB ligands exist, which are thought to activate erbB receptors by inducing receptor hetero- as well as homo-dimerization. A view has emerged in which each ligand induces a specific set of receptor homo- and hetero-dimers, which yield characteristic biological responses. We have set about quantitating the ability of erbB ligands to induce specific erbB receptor dimer using purified isolated receptor extracellular domains.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 01, 1999
- Accession Number
- ADB258643
Entities
People
- Mark A. Lemmon
Organizations
- University of Pennsylvania