The structure of aquaporins

1. Introduction 362 1.1 The elusive water pores 362 1.2 CHIP28 362 2. Studies on AQP-1 363 2.1 Expression of AQP1 cDNA in Xenopus oocytes 363 2.2 Reconstitution of purified AQP1 into artificial lipid bilayers 364 2.3 Structural information deduced from the primary sequence 365 2.4 Evolution and mamm...

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Bibliographic Details
Published in:Quarterly reviews of biophysics 2006-11, Vol.39 (4), p.361-396
Main Authors: Gonen, Tamir, Walz, Thomas
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Aquaporins - chemistry
Aquaporins - physiology
Aquaporins - ultrastructure
Biophysics
Cell Membrane - chemistry
Cell Membrane - physiology
Cell Membrane Permeability - physiology
Escherichia coli
Humans
Ion Channel Gating - physiology
Membranes
Molecular Sequence Data
Molecular structure
Protein Conformation
Substrates
Water
Water - chemistry
Water - metabolism
Xenopus
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Summary:1. Introduction 362 1.1 The elusive water pores 362 1.2 CHIP28 362 2. Studies on AQP-1 363 2.1 Expression of AQP1 cDNA in Xenopus oocytes 363 2.2 Reconstitution of purified AQP1 into artificial lipid bilayers 364 2.3 Structural information deduced from the primary sequence 365 2.4 Evolution and mammalian AQPs 365 3. Chronological overview over AQP structures 368 3.1 AQP1 – the red blood cell water pore 368 3.2 GlpF – the E. coli glycerol facilitator 371 3.3 AQPZ – the E. coli water pore 372 3.4 AQP0 – the lens-specific aquaporin 373 3.5 AQP4 – the main aquaporin in brain 377 3.6 SoPiP2;1 – a plant aquaporin 379 3.7 AQPM – an archaeabacterial aquaporin 379 4. Proton exclusion 380 5. Substrate selectivity 382 6. Pore regulation 385 6.1 Hormonal regulation of AQP trafficking 385 6.2 Influence of pH on AQP water conduction 386 6.3 Regulation of AQP pore conductance by protein binding 387 6.4 Pore closure by conformational changes in the AQP0 pore 388 7. Unresolved questions 390 8. Acknowledgments 390 9. References 391 The ubiquitous members of the aquaporin (AQP) family form transmembrane pores that are either exclusive for water (aquaporins) or are also permeable for other small neutral solutes such as glycerol (aquaglyceroporins). The purpose of this review is to provide an overview of our current knowledge of AQP structures and to describe the structural features that define the function of these membrane pores. The review will discuss the mechanisms governing water conduction, proton exclusion and substrate specificity, and how the pore permeability is regulated in different members of the AQP family.
ISSN:0033-5835
1469-8994
DOI:10.1017/S0033583506004458