The Single Transmembrane Domains of Human Receptor Tyrosine Kinases Encode Self-Interactions
Carmen Finger1,2*,
Claudia Escher1*, and
Dirk Schneider1
1 Institut für Biochemie und Molekularbiologie, ZBMZ, Albert-Ludwigs-Universität, Stefan-Meier-Strasse 17, 79104 Freiburg, Germany.
2 Fakultät für Biologie, Albert-Ludwigs-Universität, Stefan-Meier-Strasse 17, 79104 Freiburg, Germany.
* These authors contributed equally to this work.
Abstract:
Transmembrane signaling by receptor tyrosine kinases typically involves a dynamic receptor monomer-dimer equilibrium in which ligand binding to soluble extracellular domains triggers receptor dimerization and subsequent signaling events. Although the role in signal transduction of the single transmembrane helices of individual receptors, which connect the extracellular with the intracellular protein domains, is not understood in detail, we show here that the single transmembrane domains of all 58 human receptor tyrosine kinases alone have an intrinsic propensity to form stable dimeric structures within a membrane. Thus, defined interactions of the transmembrane domains are most likely generally involved in signaling by all human receptor tyrosine kinases.
To whom correspondence should be addressed. E-mail: Dirk.Schneider{at}biochemie.uni-freiburg.de
