Dynamic association of the intramembrane proteases SPPL2a/b and their substrates with tetraspanin-enriched microdomains
iScience, ISSN: 2589-0042, Vol: 26, Issue: 10, Page: 107819
2023
- 2Citations
- 5Captures
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Metrics Details
- Citations2
- Citation Indexes2
- Captures5
- Readers5
Article Description
Signal peptide peptidase-like 2a and b (SPPL2a/b) are aspartyl intramembrane proteases and cleave tail-anchored proteins as well as N-terminal fragments (NTFs) derived from type II-oriented transmembrane proteins. How these proteases recruit substrates and cleavage is regulated, is still incompletely understood. We found that SPPL2a/b localize to detergent-resistant membrane (DRM) domains with the characteristics of tetraspanin-enriched microdomains (TEMs). Based on this, association with several tetraspanins was evaluated. We demonstrate that not only SPPL2a/b but also their substrates tumor necrosis factor (TNF) and CD74 associate with tetraspanins like CD9, CD81, and CD82 and/or TEMs and analyze the stability of these complexes in different detergents. CD9 and CD81 deficiency has protease- and substrate-selective effects on SPPL2a/b function. Our findings suggest that reciprocal interactions with tetraspanins may assist protease-substrate encounters of SPPL2a/b within the membrane. Beyond SPP/SPPL proteases, this supports previous concepts that tetraspanins facilitate membrane-embedded proteolytic processes.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S2589004223018965; http://dx.doi.org/10.1016/j.isci.2023.107819; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85171353078&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/37736044; https://linkinghub.elsevier.com/retrieve/pii/S2589004223018965; https://dx.doi.org/10.1016/j.isci.2023.107819
Elsevier BV
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