Structural mechanism of plant aquaporin gating

Nature - Tập 439 Số 7077 - Trang 688-694 - 2006
Susanna Törnroth‐Horsefield1, Yi Wang2, Kristina Hedfalk1, Urban Johanson3, Maria Karlsson3, Emad Tajkhorshid2, Richard Neutze1, Per Kjellbom3
1Department of Chemistry and Bioscience,Chalmers University of Technology,Göteborg,Sweden.
2Theoretical and Computational Biophysics Group, Beckman Institute, University of Illinois at Urbana-Champaign, Urbana, USA
3Dept. of Plant Biochemistry, Lund University, Lund, Sweden

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Preston, G. M., Carroll, T. P., Guggino, W. B. & Agre, P. Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science 256, 385–387 (1992)

Johansson, I., Karlsson, M., Johanson, U., Larsson, C. & Kjellbom, P. The role of aquaporins in cellular and whole plant water balance. Biochim. Biophys. Acta 1465, 324–342 (2000)

Agre, P. & Kozono, D. Aquaporin water channels: molecular mechanisms for human diseases. FEBS Lett. 555, 72–78 (2003)

King, L. S., Kozono, D. & Agre, P. From structure to disease: the evolving tale of aquaporin biology. Nature Rev. Mol. Cell Biol. 5, 687–698 (2004)

Tamas, M. J. et al. A short regulatory domain restricts glycerol transport through yeast Fps1p. J. Biol. Chem. 278, 6337–6345 (2003)

Johanson, U. et al. The complete set of genes encoding major intrinsic proteins in Arabidopsis provides a framework for a new nomenclature for major intrinsic proteins in plants. Plant Physiol. 126, 1358–1369 (2001)

Morishita, Y., Sakube, Y., Sasaki, S. & Ishibashi, K. Molecular mechanisms and drug development in aquaporin water channel diseases: aquaporin superfamily (superaquaporins): expansion of aquaporins restricted to multicellular organisms. J. Pharmacol. Sci. 96, 276–279 (2004)

Borstlap, A. C. Early diversification of plant aquaporins. Trends Plant Sci. 7, 529–530 (2002)

Johansson, I. et al. Water transport activity of the plasma membrane aquaporin PM28A is regulated by phosphorylation. Plant Cell 10, 451–459 (1998)

Johansson, I., Larsson, C., Ek, B. & Kjellbom, P. The major integral proteins of spinach leaf plasma membranes are putative aquaporins and are phosphorylated in response to Ca2+ and apoplastic water potential. Plant Cell 8, 1181–1191 (1996)

Tournaire-Roux, C. et al. Cytosolic pH regulates root water transport during anoxic stress through gating of aquaporins. Nature 425, 393–397 (2003)

Murata, K. et al. Structural determinants of water permeation through aquaporin-1. Nature 407, 599–605 (2000)

Sui, H., Han, B. G., Lee, J. K., Walian, P. & Jap, B. K. Structural basis of water-specific transport through the AQP1 water channel. Nature 414, 872–878 (2001)

Savage, D. F., Egea, P. F., Robles-Colmenares, Y., O'Connell, J. D. & Stroud, R. M. Architecture and selectivity in aquaporins: 2.5 Å X-ray structure of aquaporin Z. PLoS Biol. 1, E72 (2003)

Gonen, T., Sliz, P., Kistler, J., Cheng, Y. & Walz, T. Aquaporin-0 membrane junctions reveal the structure of a closed water pore. Nature 429, 193–197 (2004)

Harries, W. E., Akhavan, D., Miercke, L. J., Khademi, S. & Stroud, R. M. The channel architecture of aquaporin 0 at a 2.2 Å resolution. Proc. Natl Acad. Sci. USA 101, 14045–14050 (2004)

Fu, D. et al. Structure of a glycerol-conducting channel and the basis for its selectivity. Science 290, 481–486 (2000)

Tajkhorshid, E. et al. Control of the selectivity of the aquaporin water channel family by global orientational tuning. Science 296, 525–530 (2002)

de Groot, B. L. & Grubmuller, H. Water permeation across biological membranes: mechanism and dynamics of aquaporin-1 and GlpF. Science 294, 2353–2357 (2001)

Jensen, M. O., Tajkhorshid, E. & Schulten, K. The mechanism of glycerol conduction in aquaglyceroporins. Structure 9, 1083–1093 (2001)

Jensen, M. O., Park, S., Tajkhorshid, E. & Schulten, K. Energetics of glycerol conduction through aquaglyceroporin GlpF. Proc. Natl Acad. Sci. USA 99, 6731–6736 (2002)

Daniels, M. J., Chrispeels, M. J. & Yeager, M. Projection structure of a plant vacuole membrane aquaporin by electron cryo-crystallography. J. Mol. Biol. 294, 1337–1349 (1999)

Kukulski, W. et al. The 5 Å structure of heterologously expressed plant aquaporin SoPIP2;1. J. Mol. Biol. 350, 611–616 (2005)

Hedges, S. B., Blair, J. E., Venturi, M. L. & Shoe, J. L. A molecular timescale of eukaryote evolution and the rise of complex multicellular life. BMC Evol. Biol. 4, 2 (2004)

Jung, J. S., Preston, G. M., Smith, B. L., Guggino, W. B. & Agre, P. Molecular structure of the water channel through aquaporin CHIP. The hourglass model. J. Biol. Chem. 269, 14648–14654 (1994)

Wang, Y., Schulten, K. & Tajkhorshid, E. What makes an aquaporin a glycerol channel: A comparative study of AqpZ and GlpF. Structure 13, 1107–1118 (2005)

de Groot, B. L., Frigato, T., Helms, V. & Grubmuller, H. The mechanism of proton exclusion in the aquaporin-1 water channel. J. Mol. Biol. 333, 279–293 (2003)

Jensen, M. O., Tajkhorshid, E. & Schulten, K. Electrostatic tuning of permeation and selectivity in aquaporin water channels. Biophys. J. 85, 2884–2899 (2003)

Chakrabarti, N., Tajkhorshid, E., Roux, B. & Pomes, R. Molecular basis of proton blockage in aquaporins. Structure 12, 65–74 (2004)

Ilan, B., Tajkhorshid, E., Schulten, K. & Voth, G. A. The mechanism of proton exclusion in aquaporin channels. Proteins 55, 223–228 (2004)

de Groot, B. L. & Grubmüller, H. The dynamics and energetics of water permeation and proton exclusion in aquaporins. Curr. Opin. Struct. Biol. 15, 176–183 (2005)

Smart, O. S., Goodfellow, J. M. & Wallace, B. A. The pore dimensions of gramicidin A. Biophys. J. 65, 2455–2460 (1993)

Nemeth-Cahalan, K. L. & Hall, J. E. pH and calcium regulate the water permeability of aquaporin 0. J. Biol. Chem. 275, 6777–6782 (2000)

Zelenina, M., Bondar, A. A., Zelenin, S. & Aperia, A. Nickel and extracellular acidification inhibit the water permeability of human aquaporin-3 in lung epithelial cells. J. Biol. Chem. 278, 30037–30043 (2003)

Zelenina, M., Tritto, S., Bondar, A. A., Zelenin, S. & Aperia, A. Copper inhibits the water and glycerol permeability of aquaporin-3. J. Biol. Chem. 279, 51939–51943 (2004)

Madsen, D. & Kleywegt, G. J. Interactive motif and fold recognition in protein structures. J. Appl. Crystallogr. 35, 137–139 (2001)

Karlsson, M. et al. Reconstitution of water channel function of an aquaporin overexpressed and purified from Pichia pastoris. FEBS Lett. 537, 68–72 (2003)

Bailey, S. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760–763 (1994)

Morris, R. J., Perrakis, A. & Lamzin, V. S. ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol. 374, 229–244 (2003)

Brunger, A. T. et al. Crystallography and NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905–921 (1998)

Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R. & Thornton, J. M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477–486 (1996)

Jones, T. A., Zou, J.-Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110–119 (1991)

Kalé, L. et al. NAMD2: Greater scalability for parallel molecular dynamics. J. Comp. Phys. 151, 283–312 (1999)

MacKerell, A. D. et al. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B 102, 3586–3616 (1998)

Schlenkrich, M., Brickmann, J., MacKerell, A. D. & Karplus, M. in Biological Membranes: A Molecular Perspective from Computation and Experiment (eds Merz, K. M. & Roux, B.) 31–81 (Birkhauser, Boston, Massachusetts, 1996)

Darden, T., York, D. & Pedersen, L. Particle Mesh Ewald—an N.log(N) method for Ewald sums in large systems. J. Chem. Phys. 98, 10089–10092 (1993)

Humphrey, W., Dalke, A. & Schulten, K. VMD: visual molecular dynamics. J. Mol. Graph. 14, 33–38 (1996)