Reactome | gamma-secretase cleaves EPHB2

gamma-secretase cleaves EPHB2

Stable Identifier

R-HSA-3928656

Type

Reaction [omitted]

Species

Homo sapiens

Compartment

plasma membrane, cytosol

ReviewStatus

5/5

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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
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
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