gamma-secretase cleaves EPHB2

Stable Identifier
Reaction [omitted]
Homo sapiens
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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
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
16511561 Metalloproteinase/Presenilin1 processing of ephrinB regulates EphB-induced Src phosphorylation and signaling

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

EMBO J. 2006
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
Participant Of
Catalyst Activity
Catalyst Activity
endopeptidase activity of gamma-secretase complex [plasma membrane]
Physical Entity
Orthologous Events