Repository logo

Browsing by Issue Date, starting with "2017-10-17"

Filter results by year or month
Now showing 1 - 2 of 2
  • Open Science, Open Data, Open Source
    Publication . Vos, Rutger A.; Fernandes, Pedro L.
    Making research findings available free of charge for all readers has been a major challenge identified by the European Commission. Several initiatives have been made to facilitate scientific data to the community. But has science progresses, the volume of data and platforms where information can be found also increases. The task of searching for data can be overwhelming. Pedro Fernandes, IGC member and Coordinator of the GTPB - the Gulbenkian Training Programme in Bioinformatics, and Rutger Vos, from Naturalis Biodiversity Center, set to tackle this problem by creating useful information to help producing, storing, managing and finding scientific information in open resources. Their efforts resulted in 'Open Science, Open Data, Open Source - 21st century research skills for the life sciences', an e-book that can be freely used by the scientific community, policy-makers, funding agencies, among others.
    2017-10-17Book Open access Show more
  • Phosphorylation of iRhom2 Controls Stimulated Proteolytic Shedding by the Metalloprotease ADAM17/TACE
    Publication . Cavadas, Miguel; Oikonomidi, Ioanna; Gaspar, Catarina J.; Burbridge, Emma; Badenes, Marina; Félix, Inês; Bolado, Alfonso; Hu, Tianyi; Bileck, Andrea; Gerner, Christopher; Domingos, Pedro M.; von Kriegsheim, Alex; Adrain, Colin
    Cell surface metalloproteases coordinate signaling during development, tissue homeostasis, and disease. TACE (TNF-α-converting enzyme), is responsible for cleavage ("shedding") of membrane-tethered signaling molecules, including the cytokine TNF, and activating ligands of the EGFR. The trafficking of TACE within the secretory pathway requires its binding to iRhom2, which mediates the exit of TACE from the endoplasmic reticulum. An important, but mechanistically unclear, feature of TACE biology is its ability to be stimulated rapidly on the cell surface by numerous inflammatory and growth-promoting agents. Here, we report a role for iRhom2 in TACE stimulation on the cell surface. TACE shedding stimuli trigger MAP kinase-dependent phosphorylation of iRhom2 N-terminal cytoplasmic tail. This recruits 14-3-3 proteins, enforcing the dissociation of TACE from complexes with iRhom2, promoting the cleavage of TACE substrates. Our data reveal that iRhom2 controls multiple aspects of TACE biology, including stimulated shedding on the cell surface.
    2017-10-17Journal article Open access Show more