Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.7/781
Título: Quantitative proteomics screen identifies a substrate repertoire of rhomboid protease RHBDL2 in human cells and implicates it in epithelial homeostasis
Autor: Johnson, Nicholas
Březinová, Jana
Stephens, Elaine
Burbridge, Emma
Freeman, Matthew
Adrain, Colin
Strisovsky, Kvido
Palavras-chave: Proteases
Secretion
Data: 4-Ago-2017
Editora: Nature Publishing Group
Citação: Johnson, N. et al. Quantitative proteomics screen identifies a substrate repertoire of rhomboid protease RHBDL2 in human cells and implicates it in epithelial homeostasis. Sci Rep 7, 7283 (2017).
Resumo: 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.
Descrição: This deposit is composed by the main article plus the supplementary materials of the publication.
Peer review: yes
URI: http://hdl.handle.net/10400.7/781
DOI: 10.1038/s41598-017-07556-3
Versão do Editor: https://www.nature.com/articles/s41598-017-07556-3
Aparece nas colecções:MT- Artigos

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Johnson_Sci.Rep.2017_SM.pdfsupplementary material1,01 MBAdobe PDFVer/Abrir


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