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Interaction between ErbB‐1 and ErbB‐2 transmembrane domains in bilayer membranes
Author(s) -
Sharpe Simon,
Barber Kathryn R.,
Grant Chris W.M.
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02716-3
Subject(s) - transmembrane protein , erbb , transmembrane domain , lipid bilayer , receptor tyrosine kinase , oligomer , chemistry , biophysics , ligand (biochemistry) , receptor , membrane , biochemistry , biology , organic chemistry
The transmembrane domains of ErbB receptor tyrosine kinases are monotopic helical structures proposed to be capable of direct side‐to‐side contact with related receptors. Formation of the resulting homo‐ or hetero‐oligomeric complexes is considered a key step in ligand‐mediated signalling. ErbB‐2, which has not been observed to form active homo ‐dimers in a ligand dependent manner, has been implicated as an important partner for formation of hetero ‐dimers with other ErbB receptors. Recent work has shown that the ErbB‐2 transmembrane domain is capable of forming homo‐oligomeric species in lipid bilayers, while a similar domain from ErbB‐1 appears to have a lesser tendency to such interactions. Here, 2 H nuclear magnetic resonance was used to investigate the role of the ErbB‐2 transmembrane domain in hetero‐oligomerisation with that of ErbB‐1. At low total concentrations of peptide in the membrane, ErbB‐2 transmembrane domains were found to decrease the mobility of corresponding ErbB‐1 domains. The results are consistent with the existence of direct transmembrane domain involvement in hetero‐oligomer formation within the ErbB receptor family.