MMP2,9 cleave EPHB

Stable Identifier
Reaction [omitted]
Homo sapiens
Locations in the PathwayBrowser
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

Alternatively, the EPH:ephrin (EPH:EFN) interaction can be broken by proteolytic cleavage of the EPH receptors by matrix metalloproteinases (MMPs) and gamma-secretase. Ethell and his group showed that the EPHB2 receptor is cleaved by the secreted MMPs MMP-2 and MMP-9, and this cleavage is induced by EFNB:EPHB receptor interaction. EPHB2 receptor is initially cleaved within the fibronectin (FN) type III domain or between residues 543 and 544 (mouse EPHB2) at the cell surface by MMPs to produce a long fragment that is released to the extracellular space and a membrane bound C-terminal fragment (Ethell et al. 2007, Litterst et al. 2007).

Literature References
PubMed ID Title Journal Year
17428795 Ligand binding and calcium influx induce distinct ectodomain/gamma-secretase-processing pathways of EphB2 receptor

Wisniewski, T, Litterst, C, Ludwig, A, Wang, R, Georgakopoulos, A, Robakis, NK, Shioi, J, Ghersi, E

J. Biol. Chem. 2007
18713744 Ephrin-B2-induced cleavage of EphB2 receptor is mediated by matrix metalloproteinases to trigger cell repulsion

Ethell, DW, Sloniowski, S, Ethell, IM, Lin, KT

J. Biol. Chem. 2008
Catalyst Activity

serine-type endopeptidase activity of MMP2, MMP9 [extracellular region]

Orthologous Events
Cite Us!