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Open AccessJournal ArticleDOI

Insight into the Mammalian Aquaporin Interactome

TLDR
This review provides a comprehensive overview of the current knowledge of the AQP interactomes and addresses the molecular basis and functional significance of these protein–protein interactions in health and diseases.
Abstract
Aquaporins (AQPs) are a family of transmembrane water channels expressed in all living organisms. AQPs facilitate osmotically driven water flux across biological membranes and, in some cases, the movement of small molecules (such as glycerol, urea, CO2, NH3, H2O2). Protein–protein interactions play essential roles in protein regulation and function. This review provides a comprehensive overview of the current knowledge of the AQP interactomes and addresses the molecular basis and functional significance of these protein–protein interactions in health and diseases. Targeting AQP interactomes may offer new therapeutic avenues as targeting individual AQPs remains challenging despite intense efforts.

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Journal ArticleDOI

Aquaporin-5 Dynamic Regulation

TL;DR: A comprehensive overview of the current knowledge of the upstream and downstream effectors of AQP5 can be found in this paper to gain an in-depth understanding of the physiological and pathophysiological processes involving AQP-5.
Journal ArticleDOI

Involvement of aquaporin 5 in Sjögren's syndrome.

TL;DR: A review of the role of AQP5 in Sjögren's syndrome salivary gland epithelial cell dysregulation, focusing on its trafficking and protein-protein interactions is provided in this paper .
Journal ArticleDOI

Aquaporin regulates cell rounding through vacuole formation during endothelial-to-hematopoietic transition

- 01 Jun 2023 - 
TL;DR: The authors showed that large vacuoles were transiently formed in avian hemogenic endothelial cells (HECs), and aquaporin 1 (AQP1) was localized in the vacuole and plasma membranes.
Book ChapterDOI

Aquaporins in Glandular Secretion.

TL;DR: The role of aquaporins in secretory glands located within the gastrointestinal tract, including salivary glands, gastric glands, duodenal Brunner’s glands, liver, gallbladder, intestinal goblets cells, and pancreas, as well and in other parts of the body, including airway submucosal glands, lacrimal glands, mammary glands and eccrine sweat glands as mentioned in this paper .
Posted ContentDOI

Aquaporin regulates cell rounding through vacuole formation during endothelial-to-hematopoietic transition

TL;DR: These findings provide the first evidence indicating that morphological segregation of HSCs from endothelial cells is regulated by water influx into vacuoles, and provide important insights for further exploration of the mechanisms underlying cell/tissue morphogenesis through water-adoptive cellular responses.
References
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Journal ArticleDOI

Specific Aquaporins Facilitate the Diffusion of Hydrogen Peroxide across Membranes

TL;DR: Evidence that aquaporins can channel hydrogen peroxide (H2O2) through specific members of the aquaporin family is presented, the first molecular genetic evidence for the diffusion of H2 O2 through specificMembers of the Aquaporin Family is presented.
Journal ArticleDOI

Copper-Zinc Superoxide Dismutase (SOD1) Is Released by Microglial Cells and Confers Neuroprotection against 6-OHDA Neurotoxicity

TL;DR: Using proteomic analysis, SOD1, constitutively produced and released by microglia through a lysosomal secretory pathway, is identified here for the first time as an essential component of neuroprotection mediated bymicroglia.
Journal ArticleDOI

Impairment of angiogenesis and cell migration by targeted aquaporin-1 gene disruption

TL;DR: A fundamental role of water channels in cell migration, which is central to diverse biological phenomena including angiogenesis, wound healing, tumour spread and organ regeneration, is supported.
Journal ArticleDOI

Structure and function of aquaporin water channels

TL;DR: Evidence for possible movement of ions and carbon dioxide through the aquaporins is reviewed here, as well as evidence for direct regulation of aquaporin function by posttranslational modification such as phosphorylation.
Journal ArticleDOI

Lipid-protein interactions in double-layered two-dimensional AQP0 crystals

TL;DR: A 1.9 Å resolution structure of junctional AQP0 is described, determined by electron crystallography of double-layered two-dimensional crystals, which shows that junction formation depends on a conformational switch in an extracellular loop.
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