title: Activation of transmembrane cell-surface receptors via a common mechanism? The "rotation model".
abstract: It has long been thought that transmembrane cell-surface receptors, such as receptor tyrosine kinases and cytokine receptors, among others, are activated by ligand binding through ligand-induced dimerization of the receptors. However, there is growing evidence that prior to ligand binding, various transmembrane receptors have a preformed, yet inactive, dimeric structure on the cell surface. Various studies also demonstrate that during transmembrane signaling, ligand binding to the extracellular domain of receptor dimers induces a rotation of transmembrane domains, followed by rearrangement and/or activation of intracellular domains. The paper here describes transmembrane cell-surface receptors that are known or proposed to exist in dimeric form prior to ligand binding, and discusses how these preformed dimers are activated by ligand binding.
authors.affiliation: Okinawa Institute of Science and Technology Graduate University, Onna, Okinawa, Japan.
authors.forename: Ichiro N
authors.initials: IN
authors.lastname: Maruyama
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D008954:Models, Biological; D055503:Protein Multimerization; D011956:Receptors, Cell Surface / Q000378:metabolism*; D012399:Rotation
chemical_list: D008024:Ligands; D011956:Receptors, Cell Surface
keywords: cytokine; dimerization; ligand binding; preformed dimer; transmembrane signaling; tyrosine kinase