Roles of the third Ig-like domain of Necl-5/PVR and the fifth Ig-like domain of the PDGF receptor in its signaling.
Genes Cells
; 23(3): 214-224, 2018 Mar.
Article
em En
| MEDLINE
| ID: mdl-29431243
ABSTRACT
The immunoglobulin (Ig)-like cell adhesion molecule nectin-like molecule (Necl)-5/poliovirus receptor is up-regulated in many types of cancer cells and implicated in their abnormally enhanced cell proliferation and movement. We previously showed that Necl-5 cis-interacts with the platelet-derived growth factor (PDGF) receptor ß through the extracellular region and enhances its signaling. Although this cis-interaction does not affect the PDGF-induced tyrosine phosphorylation of the receptor, the interaction of the cytoplasmic region of Necl-5 with sprouty2 and the regulation of its activity are required for the enhancement of the PDGF receptor ß signaling by Necl-5. We investigated here the more detailed mechanism for this cis-interaction of Necl-5 with the PDGF receptor ß. Necl-5 contains three Ig-like domains and the PDGF receptor ß contains five Ig-like domains at their extracellular regions. We showed here that the third Ig-like domain of Necl-5 cis-interacted with the fifth Ig-like domain of the PDGF receptor ß. The recombinant protein of the third Ig-like domain of Necl-5 inhibited the cis-interaction of full-length Necl-5 with the PDGF receptor ß and the PDGF-induced activation of the ERK signaling pathway that was enhanced by Necl-5. These results revealed the novel roles of the third Ig-like domain of Necl-5 and the fifth Ig-like domain of the PDGF receptor ß in its signaling.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Receptores Virais
/
Receptor beta de Fator de Crescimento Derivado de Plaquetas
/
Domínios de Imunoglobulina
Limite:
Animals
/
Humans
Idioma:
En
Ano de publicação:
2018
Tipo de documento:
Article