title: Aquaporin gating.
abstract: An acceleration in the rate at which new aquaporin structures are determined means that structural models are now available for mammalian AQP0, AQP1, AQP2 and AQP4, bacterial GlpF, AqpM and AQPZ, and the plant SoPIP2;1. With an apparent consensus emerging concerning the mechanism of selective water transport and proton extrusion, emphasis has shifted towards the issues of substrate selectivity and the mechanisms of aquaporin regulation. In particular, recently determined structures of plant SoPIP2;1, sheep and bovine AQP0, and Escherichia coli AQPZ provide new insights into the underlying structural mechanisms by which water transport rates are regulated in diverse organisms. From these results, two distinct pictures of 'capping' and 'pinching' have emerged to describe aquaporin gating.
authors.affiliation: Chalmers University of Technology, Department of Chemistry and Bioscience, SE-405 30 Göteborg, Sweden.
authors.forename: Kristina
authors.initials: K
authors.lastname: Hedfalk
authors.forename: Susanna
authors.initials: S
authors.lastname: Törnroth-Horsefield
authors.forename: Maria
authors.initials: M
authors.lastname: Nyblom
authors.forename: Urban
authors.initials: U
authors.lastname: Johanson
authors.forename: Per
authors.initials: P
authors.lastname: Kjellbom
authors.forename: Richard
authors.initials: R
authors.lastname: Neutze
mesh_terms: D000818:Animals; D020346:Aquaporins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D006801:Humans
chemical_list: D020346:Aquaporins