Journal
BIOESSAYS
Volume 37, Issue 9, Pages 959-967Publisher
WILEY-BLACKWELL
DOI: 10.1002/bies.201500041
Keywords
cytokine; dimerization; ligand binding; preformed dimer; transmembrane signaling; tyrosine kinase
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Funding
- Okinawa Institute of Science and Technology Graduate University, Okinawa, Japan
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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.
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