gamma-secretase cleaves EPHB2

Stable Identifier
R-HSA-3928656
Type
Reaction [omitted]
Species
Homo sapiens
Compartment
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EPHB2-C-terminal fragment1 (CTF1) is subsequently cleaved within the transmembrane domain between residues 569 and 570 (mouse EPHB2) by gamma-secretase to release a shorter cytosolic fragment containing 425 C-terminal amino acids. The EPHB2 cleavage products EPHB2-CTF1 and EPHB2-CTF2 may enhance the duration of full length EPHB2 phosphorylation. These fragments lack the ephrin (EFN)-binding domain, but retain the entire cytoplasmic portion of the receptor, and may sequester phosphatases from full-length EPHB2 receptor, thus preventing its dephosphorylation (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

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

J. Biol. Chem. 2008
16511561 Metalloproteinase/Presenilin1 processing of ephrinB regulates EphB-induced Src phosphorylation and signaling

Xu, C, Baki, L, Serban, G, Litterst, C, Georgakopoulos, A, Robakis, NK, Ghersi, E

EMBO J. 2006
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
Participants
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Catalyst Activity

endopeptidase activity of gamma-secretase complex [plasma membrane]

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