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iTAP, a novel iRhom interactor, controls TNF secretion by policing the stability of iRhom/TACE
- 1.0491888 - ÚOCHB 2019 RIV GB eng J - Článek v odborném periodiku
Oikonomidi, I. - Burbridge, E. - Cavadas, M. - Sullivan, G. - Collis, Blanka - Naegele, H. - Clancy, D. - Březinová, Jana - Hu, T. - Bileck, A. - Gerner, C. - Bolado, A. - von Kriegsheim, A. - Martin, S. J. - Steinberg, F. - Stříšovský, Kvido - Adrain, C.
iTAP, a novel iRhom interactor, controls TNF secretion by policing the stability of iRhom/TACE.
eLife. Roč. 7, Jun 13 (2018), č. článku e35032. ISSN 2050-084X. E-ISSN 2050-084X
Grant CEP: GA MŠMT LO1302
Grant ostatní: EMBO(DE) 2329
Institucionální podpora: RVO:61388963
Klíčová slova: tumor necrosis factor * alpha-convertase TACE * protein 4.1 family
Obor OECD: Biochemistry and molecular biology
Impakt faktor: 7.551, rok: 2018
https://elifesciences.org/articles/35032
The apical inflammatory cytokine TNF regulates numerous important biological processes including inflammation and cell death, and drives inflammatory diseases. TNF secretion requires TACE (also called ADAM17), which cleaves TNF from its transmembrane tether. The trafficking of TACE to the cell surface, and stimulation of its proteolytic activity, depends on membrane proteins, called iRhoms. To delineate how the TNF/TACE/iRhom axis is regulated, we performed an immunoprecipitation/mass spectrometry screen to identify iRhom-binding proteins. This identified a novel protein, that we name iTAP (iRhom Tail-Associated Protein) that binds to iRhoms, enhancing the cell surface stability of iRhoms and TACE, preventing their degradation in lysosomes. Depleting iTAP in primary human macrophages profoundly impaired TNF production and tissues from iTAP KO mice exhibit a pronounced depletion in active TACE levels. Our work identifies iTAP as a physiological regulator of TNF signalling and a novel target for the control of inflammation.
Trvalý link: http://hdl.handle.net/11104/0285487
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