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Signaling by receptor tyrosine kinases (RTKs) involves ligand-induced dimerization of receptors within the plasma membrane, triggering subsequent downstream signaling events. Although the transmembrane domains play an important role in dimerization, the importance of their interactions in transmembrane signaling is not clearly understood. Here, I highlight recent research that describes the intrinsic propensity of the single transmembrane domains of all 58 human RTKs to self-interact and suggest that these interactions could be exploited for designing peptides to inhibit signaling through these receptors. Such “interceptor” peptides would be potentially valuable as therapeutic tools for treating disease symptoms caused by excessive or ectopic RTK signaling.