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Cells 2014, 3(2), 304-330; doi:10.3390/cells3020304

Mechanisms of Activation of Receptor Tyrosine Kinases: Monomers or Dimers

Information Processing Biology Unit, Okinawa Institute of Science and Technology Graduate University, 1919-1 Tancha, Onna-son, Kunigami, Okinawa 904-0495, Japan
Received: 6 March 2014 / Revised: 10 April 2014 / Accepted: 11 April 2014 / Published: 22 April 2014
(This article belongs to the Special Issue Receptor Tyrosine Kinases)
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Abstract

Receptor tyrosine kinases (RTKs) play essential roles in cellular processes, including metabolism, cell-cycle control, survival, proliferation, motility and differentiation. RTKs are all synthesized as single-pass transmembrane proteins and bind polypeptide ligands, mainly growth factors. It has long been thought that all RTKs, except for the insulin receptor (IR) family, are activated by ligand-induced dimerization of the receptors. An increasing number of diverse studies, however, indicate that RTKs, previously thought to exist as monomers, are present as pre-formed, yet inactive, dimers prior to ligand binding. The non-covalently associated dimeric structures are reminiscent of those of the IR family, which has a disulfide-linked dimeric structure. Furthermore, recent progress in structural studies has provided insight into the underpinnings of conformational changes during the activation of RTKs. In this review, I discuss two mutually exclusive models for the mechanisms of activation of the epidermal growth factor receptor, the neurotrophin receptor and IR families, based on these new insights.
Keywords: BDNF; cancer; dimerization; EGFR; IGF; ligand; NGF; phosphorylation; rotation/twist; transmembrane signaling; Trk BDNF; cancer; dimerization; EGFR; IGF; ligand; NGF; phosphorylation; rotation/twist; transmembrane signaling; Trk
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Maruyama, I.N. Mechanisms of Activation of Receptor Tyrosine Kinases: Monomers or Dimers. Cells 2014, 3, 304-330.

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