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A structural model of the iRhom-ADAM17 sheddase complex reveals functional insights into its trafficking and activity

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    SYSNO ASEP0572295
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleA structural model of the iRhom-ADAM17 sheddase complex reveals functional insights into its trafficking and activity
    Author(s) Kahveci-Tuerkoez, S. (DE)
    Blaesius, K. (DE)
    Wozniak, J. (DE)
    Rinkens, C. (DE)
    Seifert, A. (DE)
    Kašpárek, Petr (UMG-J)
    Ohm, H. (DE)
    Oltzen, S. (DE)
    Nieszporek, M. (DE)
    Schwarz, N. (DE)
    Babendreyer, A. (DE)
    Preisinger, C. (DE)
    Sedláček, Radislav (UMG-J) RID
    Ludwig, A. (DE)
    Duesterhoeft, S. (DE)
    Number of authors15
    Article number135
    Source TitleCellular and Molecular Life Sciences - ISSN 1420-682X
    Roč. 80, č. 5 (2023)
    Number of pages21 s.
    Languageeng - English
    CountryCH - Switzerland
    KeywordsiRhom ; adam17 ; Ectodomain shedding ; TNF signalling ; EGFR ligand release iRhom-ADAM17 complex structure ; iRhom homology domain
    OECD categoryBiochemistry and molecular biology
    R&D ProjectsLM2018126 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    Method of publishingOpen access
    Institutional supportUMG-J - RVO:68378050
    UT WOS000978465900001
    EID SCOPUS85156136892
    DOI10.1007/s00018-023-04783-y
    AnnotationSeveral membrane-anchored signal mediators such as cytokines (e.g. TNF alpha) and growth factors are proteolytically shed from the cell surface by the metalloproteinase ADAM17, which, thus, has an essential role in inflammatory and developmental processes. The membrane proteins iRhom1 and iRhom2 are instrumental for the transport of ADAM17 to the cell surface and its regulation. However, the structure-function determinants of the iRhom-ADAM17 complex are poorly understood. We used AI-based modelling to gain insights into the structure-function relationship of this complex. We identified different regions in the iRhom homology domain (IRHD) that are differentially responsible for iRhom functions. We have supported the validity of the predicted structure-function determinants with several in vitro, ex vivo and in vivo approaches and demonstrated the regulatory role of the IRHD for iRhom-ADAM17 complex cohesion and forward trafficking. Overall, we provide mechanistic insights into the iRhom-ADAM17-mediated shedding event, which is at the centre of several important cytokine and growth factor pathways.
    WorkplaceInstitute of Molecular Genetics
    ContactNikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217
    Year of Publishing2024
    Electronic addresshttps://link.springer.com/article/10.1007/s00018-023-04783-y
Number of the records: 1  

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