Structural models of the supramolecular organization of AQP0 and connexons in junctional microdomains

Scheuring, Simon; Buzhynskyy, Nikolay; Jaroslawski, Szymon; Gonçalves, Rui Pedro; Hite, Richard K; Walz, Thomas

doi:10.1016/j.jsb.2007.07.009

Cited by 46 publications

(47 citation statements)

References 23 publications

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“…The AQP0 4 arrays have lattice parameters of a = b = 65 Å and γ = 90°, alike the packing in junctional 2D crystals. 7,21 Connexons edge AQP0 4 arrays, sometimes separate arrays of different orientation and are non-ordered (Fig. 2a), as previously reported.…”

Section: Resultssupporting

confidence: 82%

High-Speed Atomic Force Microscopy: Cooperative Adhesion and Dynamic Equilibrium of Junctional Microdomain Membrane Proteins

Colom

Casuso

Boudier

et al. 2012

Journal of Molecular Biology

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Section: Resultssupporting

confidence: 82%

High-Speed Atomic Force Microscopy: Cooperative Adhesion and Dynamic Equilibrium of Junctional Microdomain Membrane Proteins

Colom

Casuso

Boudier

et al. 2012

Journal of Molecular Biology

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“…It is the most highly expressed membrane protein in these cells (45% by molarity of all lens fiber membrane protein in mice [170]). AQP0 tetramers assemble into large arrays in junctional microdomains [171], which dynamically associate and dissociate at the array edges, with only an estimated 1% existing as free tetramers at a given time, measured by high-speed atomic force microscopy of isolated sheep lens fiber membranes [172].…”

Section: Aqp0mentioning

confidence: 99%

Beyond water homeostasis: Diverse functional roles of mammalian aquaporins

Kitchen

Day

Salman

et al. 2015

Biochimica et Biophysica Acta (BBA) - General Subjects

129

115

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BACKGROUND: Aquaporin (AQP) water channels are best known as passive transporters of water that are vital for water homeostasis. SCOPE OF REVIEW:AQP knockout studies in whole animals and cultured cells, along with naturally occurring human mutations suggest that the transport of neutral solutes through AQPs has important physiological roles. Emerging biophysical evidence suggests that AQPs may also facilitate gas (CO2) and cation transport. AQPs may be involved in cell signalling for volume regulation and controlling the subcellular localization of other proteins by forming macromolecular complexes. This review examines the evidence for these diverse functions of AQPs as well their physiological relevance. MAJOR CONCLUSIONS:As well as being crucial for water homeostasis, AQPs are involved in physiologically important transport of molecules other than water, regulation of surface expression of other membrane proteins, cell adhesion, and signalling in cell volume regulation. GENERAL SIGNIFICANCE:Elucidating the full range of functional roles of AQPs beyond the passive conduction of water will improve our understanding of mammalian physiology in health and disease. The functional variety of AQPs makes them an exciting drug target and could provide routes to a range of novel therapies.3

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“…34,35 For two-dimensional PCF, a program into which the x and y coordinates of all complexes within an image delimited by a polygon are entered was written. The program calculates the separation vector, r, for all pairs of complexes (AB)-hence, the probability p(r) of finding a complex (B) in a distance interval of (r ± dr) from a given complex (A).…”

Section: Discussionmentioning

confidence: 99%

Quinone Pathways in Entire Photosynthetic Chromatophores of Rhodospirillum photometricum

Liu

Duquesne

Sturgis

et al. 2009

Journal of Molecular Biology

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Structural models of the supramolecular organization of AQP0 and connexons in junctional microdomains

Cited by 46 publications

References 23 publications

High-Speed Atomic Force Microscopy: Cooperative Adhesion and Dynamic Equilibrium of Junctional Microdomain Membrane Proteins

High-Speed Atomic Force Microscopy: Cooperative Adhesion and Dynamic Equilibrium of Junctional Microdomain Membrane Proteins

Beyond water homeostasis: Diverse functional roles of mammalian aquaporins

Quinone Pathways in Entire Photosynthetic Chromatophores of Rhodospirillum photometricum

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