Binding of EphrinA5 to RET receptor tyrosine kinase: An in vitro study Journal Article

Authors: Liu, Y.; Kaljunen, H.; Pavić, A.; Saarenpää, T.; Himanen, J. P.; Nikolov, D. B.; Goldman, A.
Article Title: Binding of EphrinA5 to RET receptor tyrosine kinase: An in vitro study
Abstract: Eph/Ephrin signaling pathways are crucial in regulating a large variety of physiological processes during development, such as cell morphology, proliferation, migration and axonal guidance. EphrinA (efn-A) ligands, in particular, can be activated by EphA receptors at cell-cell interfaces and have been proposed to cause reverse signaling via RET receptor tyrosine kinase. Such association has been reported to mediate spinal motor axon navigation, but conservation of the interactive signaling pathway and the molecular mechanism of the interaction are unclear. Here, we found Danio rerio efn-A5b bound to Mus musculus EphA4 with high affinity, revealing structurally and functionally conserved EphA/efn-A signaling. Interestingly, we observed no interaction between efn-A5b and RET from zebrafish, unlike earlier cell-based assays. Their lack of association indicates how complex efn-A signaling is and suggests that there may be other molecules involved in efn-A5-induced RET signaling. © 2018 Liu et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Journal Title: PLoS ONE
Volume: 13
Issue: 6
ISSN: 1932-6203
Publisher: Public Library of Science  
Date Published: 2018-06-11
Start Page: e0198291
Language: English
DOI: 10.1371/journal.pone.0198291
PROVIDER: scopus
PMCID: PMC5995387
PUBMED: 29889908
Notes: Article -- Export Date: 2 July 2018 -- Source: Scopus
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MSK Authors
  1. Dimitar B Nikolov
    70 Nikolov
  2. Juha P Himanen
    42 Himanen