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Regulated Intramembrane Proteolysis of the Interleukin-1 Receptor II by α-, β-, and γ-Secretase

Kuhn, Peer-Hendrik, Marjaux, Els, Imhof, Axel, De Strooper, Bart, Haass, Christian, Lichtenthaler, Stefan F.·2007·Journal of Biological Chemistry
DOI 10.1074/jbc.m700356200
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Abstract

Ectodomain shedding and intramembrane proteolysis of the amyloid precursor protein (APP) by alpha-, beta- and gamma-secretase are involved in the pathogenesis of Alzheimer disease (AD). Increased proteolytic processing and secretion of another membrane protein, the interleukin-1 receptor II (IL-1R2), have also been linked to the pathogenesis of AD. IL-1R2 is a decoy receptor that may limit detrimental effects of IL-1 in the brain. At present, the proteolytic processing of IL-1R2 remains little understood. Here we show that IL-1R2 can be proteolytically processed in a manner similar to APP. IL-1R2 expressed in human embryonic kidney 293 cells first undergoes ectodomain shedding in an alpha-secretase-like manner, resulting in secretion of the IL-1R2 ectodomain and the generation of an IL-1R2 C-terminal fragment. This fragment undergoes further intramembrane proteolysis by gamma-secretase, leading to the generation of the soluble intracellular domain of IL-1R2. Intramembrane cleavage of IL-1R2 was abolished by a highly specific inhibitor of gamma-secretase and was absent in mouse embryonic fibroblasts deficient in gamma-secretase activity. Surprisingly, the beta-secretase BACE1 and its homolog BACE2 increased IL-1R2 secretion resulting in C-terminal fragments nearly identical to the ones generated by the alpha-secretase-like cleavage. This suggests that both proteases may act as alternative alpha-secretase-like proteases. Importantly, BACE1 and BACE2 did not cleave several other…

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  • IL-1R2, an interleukin-1 decoy receptor, presents a mechanism for abnormal inflammation in response to changes in BACE1 activity.

    “Another BACE1 substrate, interleukin‐1 receptor II (IL‐1R2), an interleukin‐1 decoy receptor, presents a mechanism for abnormal inflammation in response to changes in BACE1 activity.”

    From BACE1: More than just a β‐secretase (2022) · cites this paper as [33]

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Metadata

Authors
Kuhn, P.-H., Marjaux, E., Imhof, A., De Strooper, B., Haass, C., & Lichtenthaler, S. F.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2007-04
Volume
282
Issue
16
Pages
11982-11995
ISSN
0021-9258
DOI
10.1074/jbc.m700356200
Cited by
120
References
3
Language
en
Licence

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