期刊
SCIENTIFIC REPORTS
卷 7, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41598-017-07556-3
关键词
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资金
- Purkyne Fellowship of the Academy of Sciences of the Czech Republic
- EMBO (Installation Grant) [2329]
- Ministry of Education, Youth and Sports of the Czech Republic [LK11206, LO1302]
- Marie Curie Career Integration Grant [304154, 618769]
- National Subvention for Development of Research Organisations [RVO: 61388963]
- Fundacao Calouste Gulbenkian
- Worldwide Cancer Research [14-1289]
- Fundacao para a Ciencia e Tecnologica (FCT) [PTDC/BEX-BCM/3015/2014]
- European Crohn's and Colitis organization (ECCO)
- COST [BM1406]
- Wellcome Trust [101035/Z/13/Z]
- Medical Research Council [MC_U105178780]
- MRC [MC_U105178780] Funding Source: UKRI
- Medical Research Council [MC_U105178780] Funding Source: researchfish
- Fundação para a Ciência e a Tecnologia [PTDC/BEX-BCM/3015/2014] Funding Source: FCT
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.
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