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Bioessays. 2015 Sep;37(9):959-67. doi: 10.1002/bies.201500041. Epub 2015 Aug 4.

Activation of transmembrane cell-surface receptors via a common mechanism? The "rotation model".

Author information

1
Okinawa Institute of Science and Technology Graduate University, Onna, Okinawa, Japan.

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.

KEYWORDS:

cytokine; dimerization; ligand binding; preformed dimer; transmembrane signaling; tyrosine kinase

PMID:
26241732
PMCID:
PMC5054922
DOI:
10.1002/bies.201500041
[Indexed for MEDLINE]
Free PMC Article

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