title: Membrane trafficking of aquaporin 1 is mediated by protein kinase C via microtubules and regulated by tonicity.
abstract: It is well-known that the rapid flow of water into and out of cells is controlled by membrane proteins called aquaporins (AQPs). However, the mechanisms that allow cells to quickly respond to a changing osmotic environment are less well established. Using GFP-AQP fusion proteins expressed in HEK293 cells, we demonstrate the reversible manipulation of cellular trafficking of AQP1. AQP1 trafficking was mediated by the tonicity of the cell environment in a specific PKC- and microtubule-dependent manner. This suggests that the increased level of water transport following osmotic change may be due a phosphorylation-dependent increase in the level of AQP1 trafficking resulting in membrane localization.
authors.affiliation: Life and Health Sciences, Aston University, Aston Triangle, Birmingham B4 7ET, UK.
authors.forename: Matthew T
authors.initials: MT
authors.lastname: Conner
authors.forename: Alex C
authors.initials: AC
authors.lastname: Conner
authors.forename: James E P
authors.initials: JE
authors.lastname: Brown
authors.forename: Roslyn M
authors.initials: RM
authors.lastname: Bill
mesh_terms: D051398:Aquaporin 1 / Q000235:genetics / Q000378:metabolism*; D002460:Cell Line; D002462:Cell Membrane / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D049452:Green Fluorescent Proteins / Q000235:genetics; D006801:Humans; D050576:Membrane Fusion Proteins / Q000235:genetics / Q000378:metabolism; D008870:Microtubules / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D009997:Osmotic Pressure / Q000502:physiology; D011493:Protein Kinase C / Q000502:physiology*; D021381:Protein Transport / Q000235:genetics / Q000502:physiology; D014867:Water / Q000378:metabolism
chemical_list: C496020:AQP1 protein, human; D050576:Membrane Fusion Proteins; D014867:Water; D051398:Aquaporin 1; D049452:Green Fluorescent Proteins; D011493:Protein Kinase C