title: Compartmentalized Ras signaling differentially contributes to phenotypic outputs.
abstract: Ras isoforms are membrane bound proteins that differentially localize to the plasma membrane and subcellular compartments within the cell. Whilst the cell surface is the main site for Ras activity the extent to which intracellular pools contribute to Ras function is debated. We have generated Ras chimeras targeting Ras to the ER, Golgi, mitochondria and endosomes to compare the capacity of each of these locations to support activity equivalent to normal Ras function. We find that all locations are capable of regulating the MAP kinase and Akt pathways. Furthermore, whilst endomembranous Ras pools show location-specific competence to support proliferation and transformation, Golgi-Ras is as potent as N-Ras.
authors.affiliation: Department of Cellular and Molecular Physiology, Institute of Translational Research, University of Liverpool, Liverpool L69 3BX, UK.
authors.forename: Veronica
authors.initials: V
authors.lastname: Aran
authors.forename: Ian A
authors.initials: IA
authors.lastname: Prior
mesh_terms: D000818:Animals; D002451:Cell Compartmentation; D004721:Endoplasmic Reticulum / Q000378:metabolism; D011992:Endosomes / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism; D051379:Mice; D008928:Mitochondria / Q000378:metabolism; D041681:NIH 3T3 Cells; D020033:Protein Isoforms / Q000032:analysis / Q000378:metabolism; D015398:Signal Transduction; D018631:ras Proteins / Q000032:analysis* / Q000378:metabolism*
chemical_list: D020033:Protein Isoforms; D018631:ras Proteins