http://www.cnr.it/ontology/cnr/individuo/prodotto/ID188582
The KDEL receptor couples to G alfaq/11 to activate Src kinases and regulate transport through the Golgi (Articolo in rivista)
- Type
- Label
- The KDEL receptor couples to G alfaq/11 to activate Src kinases and regulate transport through the Golgi (Articolo in rivista) (literal)
- Anno
- 2012-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1038/emboj.2012.134 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- M. Giannotta; C. Ruggiero; M. Grossi; J. Cancino; M. Capitani; T. Pulvirenti; G. M. L. Consoli; C. Geraci; F. Fanelli; A. Luini; M. Sallese (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
- http://www.nature.com/emboj/journal/v31/n13/full/emboj2012134a.html (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Unit of Genomic Approaches to Membrane Traffic, Department of Cellular and Translational Pharmacology, Consorzio Mario Negri Sud, Santa Maria Imbaro (CH),
Italy,
Department of Life Sciences, Institute of Protein Biochemistry, National Research Council (CNR) and Telethon Institute of Genetics and Medicine, Naples, Italy, Institute of Biomolecular Chemistry, National Research Council, Catania, Italy
Department of Chemistry, Dulbecco Telethon Institute (DTI), University of Modena e Reggio Emilia, Modena, Italy (literal)
- Titolo
- The KDEL receptor couples to G alfaq/11 to activate Src kinases and regulate transport through the Golgi (literal)
- Abstract
- Membrane trafficking involves large fluxes of cargo and membrane across separate compartments. These fluxes must be regulated by control systems to maintain homoeostasis. While control systems for other key functions such as protein folding or the cell cycle are well known, the mechanisms that control secretory transport are poorly understood. We have previously described a signalling circuit operating at the Golgi complex that regulates intra-Golgi trafficking and is initiated by the KDEL receptor (KDEL-R), a protein previously known to mediate protein recycling from the Golgi to the endoplasmic reticulum (ER). Here, we investigated the KDEL-R signalling mechanism. We show that the KDEL-R is predicted to fold like a G-protein-coupled receptor (GPCR), and that it binds and activates the heterotrimeric signalling G-protein G alpha(q/11) which, in turn, regulates transport through the Golgi complex. These findings reveal an unexpected GPCR-like mode of action of the KDEL-R and shed light on a core molecular control mechanism of intra-Golgi traffic. (literal)
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