Novel functions of inactive rhomboid proteins in immunity and disease

Journal of Leukocyte Biology
Ramasatyaveni GeesalaThorsten Maretzky

Abstract

iRhoms are related to a family of intramembrane serine proteinases called rhomboids but lack proteolytic activity. In mammals, there are two iRhoms, iRhom1 and iRhom2, which have similar domain structures and overlapping specificities as well as distinctive functions. These catalytically inactive rhomboids are essential regulators for the maturation and trafficking of the disintegrin metalloprotease ADAM17 from the endoplasmic reticulum to the cell surface, and are required for the cleavage and release of a variety of membrane-associated proteins, including the IL-6 receptor, l-selectin, TNF, and EGFR ligands. iRhom2-dependent regulation of ADAM17 function has been recently implicated in the development and progression of several autoimmune diseases including rheumatoid arthritis, lupus nephritis, as well as hemophilic arthropathy. In this review, we discuss our current understanding of iRhom biology, their implications in autoimmune pathologies, and their potential as therapeutic targets.

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Citations

Sep 8, 2020·The FEBS Journal·Colin Adrain, Miguel Cavadas
Sep 12, 2020·International Journal of Molecular Sciences·Mazin A Al-Salihi, Philipp A Lang
Dec 18, 2020·Frontiers in Cardiovascular Medicine·Ramasatyaveni GeesalaThorsten Maretzky
Jul 3, 2021·International Journal of Molecular Sciences·Neale HarrisonMichael G Tomlinson
Nov 6, 2021·Cancer Cell International·Lei WangZhi-Song Zhang

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