Membrane trafficking of aquaporin 1 is mediated by protein kinase C via microtubules and regulated by tonicity.
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.
Conner
Matthew T
MT
Life and Health Sciences, Aston University, Aston Triangle, Birmingham B4 7ET, UK.
Conner
Alex C
AC
Brown
James E P
JE
Bill
Roslyn M
RM
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
C496020:AQP1 protein, human; D050576:Membrane Fusion Proteins; D014867:Water; D051398:Aquaporin 1; D049452:Green Fluorescent Proteins; D011493:Protein Kinase C