title: Signaling initiated by the secretory compartment.
abstract: Classical signal transduction is initiated at the plasma membrane by extracellular signals and propagates to the cytosolic face of the same membrane. Multiple studies have shown that endomembranes can act as signaling platforms for this plasma-membrane-originated signaling. Recent evidence has indicated that endomembranes can also trigger their own signaling cascades that involve some of the molecular players that are classically engaged in signal transduction at the plasma membrane. Endomembrane-initiated signaling is important for synchronization of the functioning of the secretory pathway and coordination of the activities of the secretory organelles with other cellular machineries. However, these endomembrane-initiated regulatory circuits are only partially understood to date. This novel field is slowed by a lack of specific tools and the objective difficulties in the study of signal transduction of endomembrane-localized receptors, as their accessibility is limited. For example, the ligand-binding site of the KDEL receptor (that transduces endomembrane signaling) is positioned in the lumen of the Golgi complex. Here we report some approaches that are suitable for the study of endomembrane-initiated signaling.
authors.affiliation: Department of Cellular and Translational Pharmacology, Fondazione Mario Negri Sud, Unit of Genomic Approaches to Membrane Traffic, Santa Maria Imbaro (CH), Italy.
authors.forename: Carmen
authors.initials: C
authors.lastname: Ruggiero
authors.affiliation: Department of Life Sciences, Institute of Protein Biochemistry, National Research Council and Telethon Institute of Genetics and Medicine, Naples, Italy.
authors.forename: Jorge
authors.initials: J
authors.lastname: Cancino
authors.affiliation: FIRC Institute of Molecular Oncology Foundation, Milan, Italy.
authors.forename: Monica
authors.initials: M
authors.lastname: Giannotta
authors.affiliation: Department of Cellular and Translational Pharmacology, Fondazione Mario Negri Sud, Unit of Genomic Approaches to Membrane Traffic, Santa Maria Imbaro (CH), Italy. Electronic address: sallese@negrisud.it.
authors.forename: Michele
authors.initials: M
authors.lastname: Sallese
mesh_terms: D001324:Autoantigens / Q000235:genetics / Q000378:metabolism; D001692:Biological Transport; D015153:Blotting, Western; D002462:Cell Membrane / Q000378:metabolism*; D002478:Cells, Cultured; D024042:Collagen Type I / Q000235:genetics / Q000378:metabolism; D024141:Collagen Type IV / Q000235:genetics / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D005347:Fibroblasts / Q000166:cytology / Q000378:metabolism*; D031541:Fluorescence Resonance Energy Transfer; D005786:Gene Expression Regulation; D017930:Genes, Reporter; D006056:Golgi Apparatus / Q000378:metabolism*; D049452:Green Fluorescent Proteins / Q000235:genetics / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D008164:Luminescent Proteins / Q000235:genetics / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D008856:Microscopy, Fluorescence; D010766:Phosphorylation; D015398:Signal Transduction / Q000235:genetics*; D014443:Tyrosine / Q000378:metabolism; D014759:Viral Envelope Proteins / Q000235:genetics / Q000378:metabolism; D000097573:Red Fluorescent Protein
chemical_list: D001324:Autoantigens; D024042:Collagen Type I; D024141:Collagen Type IV; D049452:Green Fluorescent Proteins; D008164:Luminescent Proteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D014443:Tyrosine; D014759:Viral Envelope Proteins; D000097573:Red Fluorescent Protein; C028391:G protein, vesicular stomatitis virus; C097741:Golgin subfamily A member 2
keywords: Endomembrane-initiated signaling; Golgi complex; Immunofluorescence microscopy; KDEL receptor; Src kinases; Traffic pulse; Tyrosine phosphorylation