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Sci. Signal., 22 September 2009
Vol. 2, Issue 89, p. ra56
A Tendency to Interact
For most receptor tyrosine kinases, which have a single transmembrane domain, dimerization is necessary for transduction of the extracellular signal to the inside of the cell. Previously, the transmembrane domains of individual receptor tyrosine kinases had been shown, in some assays, to contribute to receptor dimerization. Furthermore, mutations in the transmembrane domains of some of these proteins have been associated with aberrant activation of the receptors and cancer. Finger et al. report the systematic analysis of the self-interaction propensity of each of the transmembrane domains of all 58 human receptor tyrosine kinases. When expressed as fusion proteins in a bacterial system that reports the interaction of proteins targeted to the bacterial inner membrane, all of the transmembrane domains self-interacted, suggesting that dimerization is an intrinsic property of the transmembrane domains of these signaling receptors and that transmembrane domain interactions contribute to signal transduction.
Citation: C. Finger, C. Escher, D. Schneider, The Single Transmembrane Domains of Human Receptor Tyrosine Kinases Encode Self-Interactions. Sci. Signal.2, ra56 (2009).
Structural insights into the extracellular assembly of the hematopoietic Flt3 signaling complex.
K. Verstraete, G. Vandriessche, M. Januar, J. Elegheert, A. V. Shkumatov, A. Desfosses, K. Van Craenenbroeck, D. I. Svergun, I. Gutsche, B. Vergauwen, et al. (2011)
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The Extracellular Domain of Fibroblast Growth Factor Receptor 3 Inhibits Ligand-Independent Dimerization.