Higher order structure of aquaporin-4

Nicchia, Grazia Paola; Rossi, Andrea; Mola, Maria Grazia; Pisani, Francesco; Stigliano, Cinzia; Basco, Davide; Mastrototaro, M.; Svelto, María; Frigeri, Antonio

doi:10.1016/j.neuroscience.2010.02.008

Cited by 53 publications

(49 citation statements)

References 54 publications

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“…Similar to other aquaporins, AQP4 forms tetramers when assembled in plasma membranes (117,123) (FIGURE 1D). Each tetramer will have a central pore.…”

Section: Structure Isoforms Selectivitymentioning

confidence: 87%

Physiological Roles of Aquaporin-4 in Brain

Nagelhus

Ottersen

2013

Physiological Reviews

592

520

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(AQP4) is one of the most abundant molecules in the brain and is particularly prevalent in astrocytic membranes at the blood-brain and brain-liquor interfaces. While AQP4 has been implicated in a number of pathophysiological processes, its role in brain physiology has remained elusive. Only recently has evidence accumulated to suggest that AQP4 is involved in such diverse functions as regulation of extracellular space volume, potassium buffering, cerebrospinal fluid circulation, interstitial fluid resorption, waste clearance, neuroinflammation, osmosensation, cell migration, and Ca 2ϩ signaling. AQP4 is also required for normal function of the retina, inner ear, and olfactory system. A review will be provided of the physiological roles of AQP4 in brain and of the growing list of data that emphasize the polarized nature of astrocytes.

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“…Similar to other aquaporins, AQP4 forms tetramers when assembled in plasma membranes (117,123) (FIGURE 1D). Each tetramer will have a central pore.…”

Section: Structure Isoforms Selectivitymentioning

confidence: 87%

Physiological Roles of Aquaporin-4 in Brain

Nagelhus

Ottersen

2013

Physiological Reviews

592

520

View full text Add to dashboard Cite

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“…AQP4 is the water channel protein with the highest single channel water permeability, controlling CNS water and ion homeostasis and expressed at the barriers protecting the brain at the blood and CSF interfaces (3). In particular, it is highly concentrated in the astrocyte processes forming the bloodbrain barrier and those forming the glial limitans externa and interna (3).…”

mentioning

confidence: 99%

“…In particular, it is highly concentrated in the astrocyte processes forming the bloodbrain barrier and those forming the glial limitans externa and interna (3). The plasma membrane organization of the AQP4 water channel is unique among AQPs for two reasons.…”

mentioning

confidence: 99%

“…First, all AQPs are formed by homotetramers, whereas AQP4 forms heterotetramers made of two similar isoforms, called AQP4-M1 and AQP4-M23 (4). Second, AQP4 heterotetramers further aggregate to form very well ordered supramolecular structures known as orthogonal arrays of particles (OAPs) (3,5). AQP4 aggregation of itself into OAPs serves to enhance water permeability in those cellular domains, such as the perivascular one, where this physiological need is correlated to the fluid shifts occurring and to confer a higher level of plasma membrane stability to AQP4 water channels, confined in microdomains not delimited by tight junctions such as the glial processes (6).…”

mentioning

confidence: 99%

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Identification of a Point Mutation Impairing the Binding between Aquaporin-4 and Neuromyelitis Optica Autoantibodies

Pisani

Mola

Simone

et al. 2014

Journal of Biological Chemistry

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“…The number of subunits (tetramers) per OAP can change between four and more than one hundred. AQP4 was described to occur as heterotetramers (Nicchia et al, 2010) reflecting the relative expression level of the different splice variants (M1 and M23; Neely et al, 1999, see below). The distribution of the inward rectifier potassium channel Kir 4.1 and the K + conductivity is similar to that of AQP4 and the dystrophin-dystroglycan complex (DDC) (Blake & Kröger, 2000;Amiry-Moghaddam & Ottersen, 2003;Connors et al, 2004;Nagelhus et al, 2004;Warth et al, 2005;MacAulay & Zeuthen, 2010).…”

Section: Astrocytesmentioning

confidence: 99%