Introduction of AQP6
AQP6 is an aquaporin protein, which is encoded by the AQP6 gene in humans. AQP6 is localized exclusively in intracellular membranes in renal epithelia. AQP6 is present in membrane vesicles within podocyte cell bodies and foot processes in glomeruli, while in proximal tubules, AQP6 is abundant in membrane vesicles within the subapical compartment of segment 2 and segment 3 cells. In collecting duct, AQP6 is expressed in intracellular membrane vesicles in the apical, mid, and basolateral cytoplasm of type A intercalated cells. It is documented that the asparagine residue at the contact point between the second and fifth transmembrane domains in AQP6 may function as a teeterboard needed for rapid structural oscillations during anion permeation.
|Basic Information of AQP6|
|Aliases||Aquaporin-2-like, Kidney-specific aquaporin, hKID|
|Organism||Homo sapiens (Human)|
Function ofAQP6 Membrane Protein
Because of the unique distribution in intracellular membrane vesicles in multiple types of renal epithelia, AQP6 is predicted to play various roles, not only involved in transcellular fluid absorption, but also in distinct physiologic processes such as glomerular filtration, tubular endocytosis, and acid-base metabolism. Selectively localized to the ganglion cell layer and the outer reticular layer, AQP6 plays a key role in the decrease of the retinal ganglion cells after optic nerve compression injury. In rat retinal ganglion cells, AQP6 is reported to be selectively localized to the outer plexiform layer, where AQP6 is co-localized with the glial water channel AQP4, suggesting a preferential localization of AQP6 in glial membranes. In addition, AQP6 may be a novel player in the virus-host interactions, which may lead to less severe outcomes of an infection.
Fig.1 Unique residues in AQP6 structure. (Liu, 2005)
Application of AQP6 Membrane Protein in Literature
The article proposes that AQP6 may function as a novel player in the virus-host interactions, which may lead to less severe outcomes of an infection.
This article investigates the localization of AQP6 in the rat retina and finds that AQP6 is expressed in retinal ganglion cells and Müller cells in vitro, indicating that AQP6 might participate in water and anion transport in these cells.
The authors analyze the role of AQP6 in secretory granule membranes aided by Hg2+, which is known to activate AQP6, and they assume that AQP6 permeates halide group anions as a Hg2+-sensitive anion channel in rat parotid secretory granules.
The authors investigate the localization of AQP6 in slices of the rat neural retina and they find after blue light injury of the retina, AQP6-labeled ribbon synapses disappear and a punctate AQP6 staining redistributes from the outer plexiform layer to the inner nuclear layer. So, AQP6 may be involved in the glia-mediated Osmo and ion regulation of the extracellular space.
This article reveals the expression of AQP6 in parotid acinar cells and verifies the anion transporting properties of AQP6, suggesting that AQP6 contributes to secretion of anions in parotid acinar cells.
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