Reactome | EPHAs bind EFNAs

EPHAs bind EFNAs

Stable Identifier

R-HSA-3928646

Type

Reaction [binding]

Species

Homo sapiens

Compartment

plasma membrane

Synonyms

Ephrin-A ligands interacts with EPHA receptors

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

The first step in the initiation of EPH-mediated signaling is the high affinity interaction between EPH receptors and ephrin (EFN) ligands of the same subclass located on closely opposed cell surfaces. Membrane bound EPHs bind to EFNs with high affinity and this results in the development of close contacts between the cells. This association between EPHs and EFNs on opposing cells is called trans-interaction and this close contact is required for signaling. This high affinity interaction usually result in contact-mediated repulsion. With some exceptions, the EPH receptor A-subclass (EPHA1-A8, A10) bind to the A-class ephrins (EFNA1-A4, A6). EPH and EFN initially form a 1:1 high affinity heterodimer, where ephrin inserts its extended loop into a channel at the surface of the receptor (Himanen et al. 2007, Himanen & Nikolov 2003, Himanen et al. 2001).

Literature References

PubMed ID	Title	Journal	Year
12495863	Eph signaling: a structural view Himanen, JP, Nikolov, DB	Trends Neurosci.	2003
11780069	Crystal structure of an Eph receptor-ephrin complex Lackmann, M, Henkemeyer, M, Himanen, JP, Rajashankar, KR, Nikolov, DB, Cowan, CA	Nature	2001
17928214	Cell-cell signaling via Eph receptors and ephrins Saha, N, Himanen, JP, Nikolov, DB	Curr. Opin. Cell Biol.	2007
19525919	Ligand recognition by A-class Eph receptors: crystal structures of the EphA2 ligand-binding domain and the EphA2/ephrin-A1 complex Guo, H, Miao, H, Wang, B, Nguyen, M, Rajashankar, KR, Nikolov, DB, Buck, M, Goldgur, Y, Myshkin, E, Himanen, JP	EMBO Rep.	2009