Aquaporin gating |
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| Authors: | Hedfalk Kristina Törnroth-Horsefield Susanna Nyblom Maria Johanson Urban Kjellbom Per Neutze Richard |
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| Affiliation: | 1. Department of Pediatrics, Loma Linda University School of Medicine, Loma Linda, CA 92354, USA;2. Department of Physiology, Loma Linda University School of Medicine, Loma Linda, CA 92354, USA;3. INSERM U1049 Neuroinflammation, Imagerie et Thérapie de la Sclérose en Plaques, F-33076 Bordeaux, France;4. Univ Bordeaux, CNRS UMR 5287, 146 rue Leo Saignat33076 Bordeaux cedex;1. Université catholique de Louvain, Institut des Sciences de la Vie, Croix du Sud, 4-L7.07.14, 1348 Louvain-la-Neuve, Belgium;2. Leibniz Institute of Plant Genetics and Crop Plant Research, Corrensstrasse 3, 06466 Gatersleben, Germany |
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| 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. |
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