title: Osmotically induced cell volume changes alter anterograde and retrograde transport, Golgi structure, and COPI dissociation.
abstract: Physiological conditions that impinge on constitutive traffic and affect organelle structure are not known. We report that osmotically induced cell volume changes, which are known to occur under a variety of conditions, rapidly inhibited endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells. Both ER export and ER Golgi intermediate compartment (ERGIC)-to-Golgi trafficking steps were blocked, but retrograde transport was active, and it mediated ERGIC and Golgi collapse into the ER. Extensive tubulation and relatively rapid Golgi resident redistribution were observed under hypo-osmotic conditions, whereas a slower redistribution of the same markers, without apparent tubulation, was observed under hyperosmotic conditions. The osmotic stress response correlated with the perturbation of COPI function, because both hypo- and hyperosmotic conditions slowed brefeldin A-induced dissociation of betaCOP from Golgi membranes. Remarkably, Golgi residents reemerged after several hours of sustained incubation in hypotonic or hypertonic medium. Reemergence was independent of new protein synthesis but required PKC, an activity known to mediate cell volume recovery. Taken together these results indicate the existence of a coupling between cell volume and constitutive traffic that impacts organelle structure through independent effects on anterograde and retrograde flow and that involves, in part, modulation of COPI function.
authors.affiliation: Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA. thl@andrew.cmu.edu
authors.forename: T H
authors.initials: TH
authors.lastname: Lee
authors.forename: A D
authors.initials: AD
authors.lastname: Linstedt
mesh_terms: D000222:Adaptation, Physiological; D000818:Animals; D001692:Biological Transport; D020126:Brefeldin A / Q000494:pharmacology; D019556:COS Cells / Q000378:metabolism; D002451:Cell Compartmentation; D048429:Cell Size / Q000502:physiology*; D020756:Coatomer Protein; D004721:Endoplasmic Reticulum / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism* / Q000648:ultrastructure*; D006367:HeLa Cells / Q000378:metabolism; D006801:Humans; D006982:Hypertonic Solutions; D007038:Hypotonic Solutions; D007425:Intracellular Membranes / Q000378:metabolism; D037241:Mannose-Binding Lectins; D008565:Membrane Proteins / Q000187:drug effects / Q000378:metabolism*; D008869:Microtubule-Associated Proteins / Q000378:metabolism; D009997:Osmotic Pressure; D011493:Protein Kinase C / Q000378:metabolism; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology
chemical_list: D020756:Coatomer Protein; D006982:Hypertonic Solutions; D007038:Hypotonic Solutions; C084004:LMAN1 protein, human; D037241:Mannose-Binding Lectins; D008565:Membrane Proteins; D008869:Microtubule-Associated Proteins; D011500:Protein Synthesis Inhibitors; D020126:Brefeldin A; D011493:Protein Kinase C