The NPC Motif of Aquaporin-11, Unlike the NPA Motif of Known Aquaporins, Is Essential for Full Expression of Molecular Function

Ikeda, Masahiro; Andoo, Ayaka; Shimono, Mariko; Takamatsu, Natsuko; Taki, Asaka; Muta, Kanako; Matsushita, Wataru; Uechi, Tamayo; Matsuzaki, Toshiyuki; Kenmochi, Naoya; Takata, Kuniaki; Sasaki, Sei; Ito, Katsuaki; Ishibashi, Keiichiro

doi:10.1074/jbc.m110.180968

Cited by 75 publications

(64 citation statements)

References 33 publications

(52 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The highly preserved asparagine-proline-alanine (NPA)-motif prevents ions to pass the channel [19] and the constrictive site where an aromatic/arginine region re-positions the water molecules, letting H2O pass while excluding protons [20]. AQP11 and AQP12 are however exceptions to the presence of the conserved NPA-motif [21,22]. Under normal physiological conditions the body utilizes the AQPs for diverse organ and cellular events.…”

Section: Aquaporinsmentioning

confidence: 99%

Aquaporins in Infection and Inflammation

Holm¹

2016

Linköping University Medical Dissertations

View full text Add to dashboard Cite

About the cover:The front cover displays a human, blood-derived macrophage stained for aquaporin 9.During the course of the research underlying this thesis, Angelika Holm was enrolled in Forum Scientium, a multidisciplinary doctoral programme at Linköping University Printed by LiU-Tryck, Linköping, Sweden, 2016 "Be brave, even if you're not, pretend to be. No one can tell the difference."To that young, awkward, tall girl who dared to dream of something else, something more:You did it. SUPERVISOR Elena VikströmDepartment of Clinical and Experimental Medicine Linköping University Linköping Sweden When cells of the innate immune system encounter pathogens they need to respond and prepare for migration and phagocytosis and do so through volume regulatory processes. The Gramnegative bacterium Pseudomonas aeruginosa utilizes a small molecule-based communication system, called quorum sensing (QS) to control the production of its virulence factors and biofilms. We found that P. aeruginosa with a complete QS system elicits a stronger phagocytic response in human blood-derived macrophages compared to its lasI-/rhlI-mutant lacking the production of the QS molecules N-butyryl-L-homoserine lactone (C4-HSL) and N-3-oxododecanoyl-L-homoserine lactone (3O-C12-HSL). Infection with P. aeruginosa further increases the expression of AQP9 and induces re-localisation of AQP9 to the front and trailing ends of macrophages. Moreover, the 3O-C12-HSL alone elevates the expression of AQP9, redistribute the water channel to the front and rear ends and increases the cell area and volume of macrophages. Both infection with the wild type P. aeruginosa and the treatment with 3O-C12-HSL change the nano-structural architecture of the AQP9 distribution in macrophages. ASSISTANT SUPERVISORS Karl-Eric MagnussonViruses use the intracellular machinery of the invaded cells to produce and assemble new viral bodies. Intracellular AQPs are localised in a membranes of cellular organelles to regulate their function and morphology. C3H10T1/2 fibroblasts transiently expressing green fluorescent protein (GFP)-AQP6 show a reduced expression of AQP6 after Hazara virus infection and an increased cell area. Overexpressing AQP6 in C3H10T1/2 cells reduces the infectivity of Hazara virus indicating that AQP6 expression has a protective role in virus infections.Ion and water channels in the epithelial cell lining tightly regulate the water homeostasis. In microscopic colitis (MC), patients suffer from severe watery diarrhoeas. For the first time, we have shown that the expression of AQP1, 8 and 11 and the sodium/hydrogen exchanger NHE1 are reduced in colonic biopsies from MC patients compared to healthy control individuals. Following treatment with the glucocorticoid budesonide the patients experienced a rapid recovery and we observed a restored or increased expression of the AQPs and NHE1 during treatment, suggesting a role for AQPs in the diarrhoeal mechanisms in MC.Taken together, this thesis provides new evidence on the importance of water homeostasis regulatio...

show abstract

Section: Aquaporinsmentioning

confidence: 99%

Aquaporins in Infection and Inflammation

Holm¹

2016

Linköping University Medical Dissertations

View full text Add to dashboard Cite

show abstract

“…In rat, AQP11 also has a broad tissue distribution (Ishibashi et al, 2000b) and is localized intracellularly, most likely in association with the endoplasmic reticulum and derived vesicles with a suspected role in vesicular or vacuolar water transport . Morpholino knock-down of aqp11 in developing zebrafish embryos causes malformation of the normal linear body shape (Ikeda et al, 2011), suggesting a crucial role in morphogenesis.…”

Section: Research Articlementioning

confidence: 99%

Aquaporin expression in the Japanese medaka (Oryzias latipes, Temminck & Schlegel) in FW and SW: challenging the paradigm for intestinal water transport?

Madsen

Bujak

Tipsmark

2014

Journal of Experimental Biology

View full text Add to dashboard Cite

We investigated the salinity-dependent expression dynamics of seven aquaporin paralogs (aqp1a, aqp3a, aqp7, aqp8ab, aqp10a, aqp10b and aqp11a) in several tissues of euryhaline Japanese medaka (Oryzias latipes). All paralogs except aqp7 and aqp10a had a broad tissue distribution, and several were affected by salinity in both osmoregulatory and non-osmoregulatory tissues. In the intestine, aqp1a, aqp7, aqp8ab and aqp10a decreased upon seawater (SW) acclimation in both long-term acclimated fish and during 1-3 days of the transition period. In the gill, aqp3a was lower and aqp10a higher in SW than in freshwater (FW). In the kidney no aqps were affected by salinity. In the skin, aqp1a and aqp3a were lower in SW than in FW. In the liver, aqp8ab and aqp10a were lower in SW than in FW. Furthermore, six Na + ,K + -ATPase α-subunit isoform transcripts were analysed in the intestine but none showed a consistent response to salinity, suggesting that water transport is not regulated at this level. In contrast, mRNA of the Na + ,K + ,2Cl --cotransporter type-2 strongly increased in the intestine in SW compared with FW fish. Using custom-made antibodies, Aqp1a, Aqp8ab and Aqp10a were localized in the apical region of enterocytes of FW fish. Apical staining intensity strongly decreased, vanished or moved to subapical regions, when fish were acclimated to SW, supporting the lower mRNA expression in SW. Western blots confirmed the decrease in Aqp1a and Aqp10a in SW. The strong decrease in aquaporin expression in the intestine of SW fish is surprising, and challenges the paradigm for transepithelial intestinal water absorption in SW fishes.

show abstract

“…AQPs 11 and 12 are thought to function as water channels but have yet to be fully characterised (Ishibashi, 2009). Notably, the sequence of the NPA motifs within AQP11 and 12 deviates from the conserved NPA of the other AQPs (Ikeda et al, 2010, Itoh et al, 2005.…”

Section: Structure and Function Of Aqpsmentioning

confidence: 99%

“…AQP11 and 12 appear to lack the conserved NPA motifs, being NPC and NPT in AQPs 11 (Ikeda et al, 2010) and 12 (Itoh et al, 2005), respectively. Interestingly mutation of the alanine of the AQP4 NPA motif to threonine to mimic AQP12 resulted in retention within the endoplasmic reticulum of mammalian cell lines, whereas mutation of this alanine to cysteine, mimicking AQP11, expresses normally in plasma membrane (Guan et al, 2010).…”

Section: Localisation and Retention Signalsmentioning

confidence: 99%

An emerging consensus on aquaporin translocation as a regulatory mechanism

Conner

Bill

Conner

2012

Molecular Membrane Biology

View full text Add to dashboard Cite

Water can pass through the cell membrane relatively slowly by diffusion. However, in order to maintain water homeostasis, the rapid and specific regulation of cellular water flow is mediated by the aquaporin (AQP) family of membrane protein water channels. Thirteen human AQPs have been identified to date and the majority are highly specific for water while others show selectivity for water, glycerol and other small solutes. The wide range of tissues that are known to express AQPs is reflected by their involvement in many physiological processes and diseases. Receptor mediated translocation, via hormone activation, is an established method of AQP regulation, especially for AQP2. There is now an emerging consensus that the rapid and reversible translocation of other AQPs from intracellular vesicles to the plasma membrane, triggered by a range of stimuli, can confer increased membrane permeability. This review examines new advances that have identified molecular mechanisms of AQP regulation; these include the role of cytoskeletal proteins, kinases, calcium and retention or localisation signals as well as specific triggers of AQP translocation. This article reviews current knowledge of AQP regulation with a focus on rapid and dynamic regulation of sub-cellular AQP translocation in response to a specific trigger.3

show abstract

The NPC Motif of Aquaporin-11, Unlike the NPA Motif of Known Aquaporins, Is Essential for Full Expression of Molecular Function

Cited by 75 publications

References 33 publications

Aquaporins in Infection and Inflammation

Aquaporins in Infection and Inflammation

Aquaporin expression in the Japanese medaka (Oryzias latipes, Temminck & Schlegel) in FW and SW: challenging the paradigm for intestinal water transport?

An emerging consensus on aquaporin translocation as a regulatory mechanism

Contact Info

Product

Resources

About