MMP2,9 cleave EPHB

Stable Identifier
R-HSA-3928657
Type
Reaction [omitted]
Species
Homo sapiens
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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
18713744 Ephrin-B2-induced cleavage of EphB2 receptor is mediated by matrix metalloproteinases to trigger cell repulsion

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

J. Biol. Chem. 2008
17428795 Ligand binding and calcium influx induce distinct ectodomain/gamma-secretase-processing pathways of EphB2 receptor

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

J. Biol. Chem. 2007
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Catalyst Activity
Title
serine-type endopeptidase activity of MMP2, MMP9 [extracellular region]
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Orthologous Events
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