Finger Carmen, Escher Claudia, Schneider Dirk
Institut für Biochemie und Molekularbiologie, ZBMZ, Albert-Ludwigs-Universität, Freiburg, Germany.
Sci Signal. 2009 Sep 22;2(89):ra56. doi: 10.1126/scisignal.2000547.
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.
受体酪氨酸激酶介导的跨膜信号传导通常涉及一种动态的受体单体 - 二聚体平衡，其中配体与可溶性细胞外结构域的结合会触发受体二聚化及随后的信号传导事件。尽管连接细胞外与细胞内蛋白质结构域的各个受体的单个跨膜螺旋在信号转导中的作用尚未完全明确，但我们在此表明，所有58种人类受体酪氨酸激酶的单个跨膜结构域本身就具有在膜内形成稳定二聚体结构的内在倾向。因此，跨膜结构域的特定相互作用很可能普遍参与了所有人类受体酪氨酸激酶的信号传导。
