Article abstract
Nature Cell Biology
Published online: 20 July 2008 | doi:10.1038/ncb1751
A traffic-activated Golgi-based signalling circuit coordinates the secretory pathway
Teodoro Pulvirenti1,3,4, Monica Giannotta1,4, Mariagrazia Capestrano1, Mirco Capitani1, Antonio Pisanu1, Roman S. Polishchuk1, Enrica San Pietro1, Galina V. Beznoussenko1, Alexander A. Mironov1, Gabriele Turacchio1, Victor W. Hsu2, Michele Sallese1,5 & Alberto Luini1,5
Abstract
As with other complex cellular functions, intracellular membrane transport involves the coordinated engagement of a series of organelles and machineries; however, the molecular basis of this coordination is unknown. Here we describe a Golgi-based signalling system that is activated by traffic and is involved in monitoring and balancing trafficking rates into and out of the Golgi complex. We provide evidence that the traffic signal is due to protein chaperones that leave the endoplasmic reticulum and reach the Golgi complex where they bind to the KDEL receptor. This initiates a signalling reaction that includes the activation of a Golgi pool of Src kinases and a phosphorylation cascade that in turn activates intra-Golgi trafficking, thereby maintaining the dynamic equilibrium of the Golgi complex. The concepts emerging from this study should help to understand the control circuits that coordinate high-order cellular functions.
- Laboratory of Membrane Traffic, Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, 66030 Santa Maria Imbaro (Chieti), Italy.
- Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, and Department of Medicine, Harvard Medical School, Boston, MA 02115, USA.
- Current address: Cell Biology Program, Sloan-Kettering Institute for Cancer Research, Memorial Sloan-Kettering Cancer Center, New York, NY 90021, USA.
- These authors contributed equally to this work.
- These principal investigators contributed equally to this work
Correspondence to: Alberto Luini1,5 e-mail: luini@negrisud.it
Correspondence to: Michele Sallese1,5 e-mail: sallese@negrisud.it