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Quantitative proteomics screen identifies a substrate repertoire of rhomboid protease RHBDL2 in human cells and implicates it in epithelial homeostasis

N. Johnson, J. Březinová, E. Stephens, E. Burbridge, M. Freeman, C. Adrain, K. Strisovsky,

. 2017 ; 7 (1) : 7283. [pub] 20170804

Jazyk angličtina Země Anglie, Velká Británie

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc19013104

Rhomboids are intramembrane serine proteases conserved in all kingdoms of life. They regulate epidermal growth factor receptor signalling in Drosophila by releasing signalling ligands from their transmembrane tethers. Their functions in mammals are poorly understood, in part because of the lack of endogenous substrates identified thus far. We used a quantitative proteomics approach to investigate the substrate repertoire of rhomboid protease RHBDL2 in human cells. We reveal a range of novel substrates that are specifically cleaved by RHBDL2, including the interleukin-6 receptor (IL6R), cell surface protease inhibitor Spint-1, the collagen receptor tyrosine kinase DDR1, N-Cadherin, CLCP1/DCBLD2, KIRREL, BCAM and others. We further demonstrate that these substrates can be shed by endogenously expressed RHBDL2 and that a subset of them is resistant to shedding by cell surface metalloproteases. The expression profiles and identity of the substrates implicate RHBDL2 in physiological or pathological processes affecting epithelial homeostasis.

Citace poskytuje Crossref.org

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$a Březinová, Jana $u Institute of Organic Chemistry and Biochemistry, Czech Academy of Science, Flemingovo n. 2, Prague, 166 10, Czech Republic. Department of Biochemistry, Faculty of Science, Charles University, Prague, Czech Republic.
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$a Stephens, Elaine $u MRC Laboratory of Molecular Biology, Cambridge, CB2 2QH, United Kingdom.
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$a Burbridge, Emma $u Instituto Gulbenkian de Ciência, Lisbon, Portugal.
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$a Freeman, Matthew $u MRC Laboratory of Molecular Biology, Cambridge, CB2 2QH, United Kingdom. Sir William Dunn School of Pathology, Oxford, OX1 3RE, United Kingdom.
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$a Adrain, Colin $u Instituto Gulbenkian de Ciência, Lisbon, Portugal. cadrain@igc.gulbenkian.pt.
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$a Strisovsky, Kvido $u Institute of Organic Chemistry and Biochemistry, Czech Academy of Science, Flemingovo n. 2, Prague, 166 10, Czech Republic. kvido.strisovsky@uochb.cas.cz.
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