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Volumn 60, Issue 7, 2008, Pages 430-436

Electron crystallography of aquaporins

Author keywords

Aquaporin; Channel; Electron crystallography; Lipid protein interactions; Membrane junction

Indexed keywords

AQUAPORIN 1; AQUAPORIN 4; AQUAPORIN; LIPID; PROTEIN; WATER;

EID: 48849105126     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.53     Document Type: Review
Times cited : (12)

References (33)
  • 1
    • 0027431432 scopus 로고
    • Aquaporins: A family of water channel proteins
    • Agre, P., Sasaki, S., and Chrispeels, M. J. (1993) Aquaporins: a family of water channel proteins. Am. J. Physiol. 265, F461.
    • (1993) Am. J. Physiol. , vol.265
    • Agre, P.1    Sasaki, S.2    Chrispeels, M.J.3
  • 2
    • 0242573122 scopus 로고    scopus 로고
    • Aquaporin water channels: Molecular mechanisms for human diseases
    • DOI 10.1016/S0014-5793(03)01083-4
    • Agre, P. and Kozono, D. (2003) Aquaporin water channels: molecular mechanisms for human diseases. FEBS Lett. 555, 72-78. (Pubitemid 37431100)
    • (2003) FEBS Letters , vol.555 , Issue.1 , pp. 72-78
    • Agre, P.1    Kozono, D.2
  • 3
    • 0030922070 scopus 로고    scopus 로고
    • Water and glycerol permeabilities of aquaporins 1-5 and MIP determined quantitatively by expression of epitope-tagged constructs in Xenopus oocytes
    • Yang, B. and Verkman, A. S. (1997) Water and glycerol permeabilities of aquaporins 1-5 and MIP determined quantitatively by expression of epitope-tagged constructs in Xenopus oocytes. J. Biol. Chem. 272, 16140-16146.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16140-16146
    • Yang, B.1    Verkman, A.S.2
  • 4
    • 33845669996 scopus 로고    scopus 로고
    • The structure of aquaporins
    • Gonen, T. and Walz, T. (2006) The structure of aquaporins. Q. Rev. Biophys. 39, 361-396.
    • (2006) Q. Rev. Biophys. , vol.39 , pp. 361-396
    • Gonen, T.1    Walz, T.2
  • 5
    • 1942521362 scopus 로고    scopus 로고
    • Improved specimen preparation for cryo-electron microscopy using a symmetric carbon sandwich technique
    • Gyobu, N., Tani, K., Hiroaki, Y., Kamegawa, A., Mitsuoka, K., and Fujiyoshi, Y. (2004) Improved specimen preparation for cryo-electron microscopy using a symmetric carbon sandwich technique. J. Struct. Biol. 146, 325-333.
    • (2004) J. Struct. Biol. , vol.146 , pp. 325-333
    • Gyobu, N.1    Tani, K.2    Hiroaki, Y.3    Kamegawa, A.4    Mitsuoka, K.5    Fujiyoshi, Y.6
  • 6
    • 0031700068 scopus 로고    scopus 로고
    • The structural study of membrane proteins by electron crystallography
    • Fujiyoshi, Y. (1998) The structural study of membrane proteins by electron crystallography. Adv. Biophys. 35, 25-80.
    • (1998) Adv. Biophys. , vol.35 , pp. 25-80
    • Fujiyoshi, Y.1
  • 7
    • 2442659197 scopus 로고    scopus 로고
    • Aquaporin-0 membrane junctions reveal the structure of a closed water pore
    • DOI 10.1038/nature02503
    • Gonen, T., Sliz, P., Kistler, J., Cheng, Y., and Walz, T. (2004) Aquaporin-0 membrane junctions reveal the structure of a closed water pore. Nature 429, 193-197. (Pubitemid 38656196)
    • (2004) Nature , vol.429 , Issue.6988 , pp. 193-197
    • Gonen, T.1    Silz, P.2    Kistler, J.3    Cheng, Y.4    Walz, T.5
  • 9
    • 28444450878 scopus 로고    scopus 로고
    • Lipid-protein interactions in double-layered two-dimensional crystals of aquaporin-0
    • Gonen, T., Cheng, Y., Sliz, P., Hiroaki, Y., Fujiyoshi, Y., Harrison, S. C., and Walz, T. (2005) Lipid-protein interactions in double-layered two-dimensional crystals of aquaporin-0. Nature 438, 633-638.
    • (2005) Nature , vol.438 , pp. 633-638
    • Gonen, T.1    Cheng, Y.2    Sliz, P.3    Hiroaki, Y.4    Fujiyoshi, Y.5    Harrison, S.C.6    Walz, T.7
  • 10
    • 0031858060 scopus 로고    scopus 로고
    • 2D crystallization of membrane proteins: Rationales and examples
    • Hasler, L., Heymann, J. B., Engel, A., Kistler, J., and Walz, T. (1998) 2D crystallization of membrane proteins: rationales and examples. J. Struct. Biol. 121, 162-171.
    • (1998) J. Struct. Biol. , vol.121 , pp. 162-171
    • Hasler, L.1    Heymann, J.B.2    Engel, A.3    Kistler, J.4    Walz, T.5
  • 11
    • 0035979768 scopus 로고    scopus 로고
    • Two-dimensional crystals: A powerful approach to assess structure, function and dynamics of membrane proteins
    • Stahlberg, H., Fotiadis, D., Scheuring, S., Rémigy, H., Braun, T., Mitsuoka, K., Fujiyoshi, Y., and Engel, A. (2001) Two-dimensional crystals: a powerful approach to assess structure, function and dynamics of membrane proteins. FEBS Lett. 504, 166-172.
    • (2001) FEBS Lett. , vol.504 , pp. 166-172
    • Stahlberg, H.1    Fotiadis, D.2    Scheuring, S.3    Rémigy, H.4    Braun, T.5    Mitsuoka, K.6    Fujiyoshi, Y.7    Engel, A.8
  • 12
    • 0026503030 scopus 로고
    • Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein
    • Preston, G. M., Carroll, T. P., Guggino, W. B., and Agre, P. (1992) Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science 256, 385-387.
    • (1992) Science , vol.256 , pp. 385-387
    • Preston, G.M.1    Carroll, T.P.2    Guggino, W.B.3    Agre, P.4
  • 14
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through the AQP1 water channel
    • Sui, H., Han, B. G., Lee, J. K., Walian, P., and Jap, B. K. (2001) Structural basis of water-specific transport through the AQP1 water channel. Nature 414, 872-878.
    • (2001) Nature , vol.414 , pp. 872-878
    • Sui, H.1    Han, B.G.2    Lee, J.K.3    Walian, P.4    Jap, B.K.5
  • 16
    • 0028365632 scopus 로고
    • Functional independence of monomeric CHIP28 water channels revealed by expression of wild-type mutant heterodimers
    • Shi, L. B., Skach, W. R., and Verkman, A. S. (1994) Functional independence of monomeric CHIP28 water channels revealed by expression of wild-type mutant heterodimers. J. Biol. Chem. 269, 10417-10422.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10417-10422
    • Shi, L.B.1    Skach, W.R.2    Verkman, A.S.3
  • 18
    • 0030011088 scopus 로고    scopus 로고
    • Structure and dynamics of a proton wire: A theoretical study of H1 translocation along the single-file water chain in the gramicidin a channel
    • Pomes, R. and Roux, B. (1996) Structure and dynamics of a proton wire: a theoretical study of H1 translocation along the single-file water chain in the gramicidin A channel. Biophys. J. 71, 19-39.
    • (1996) Biophys. J. , vol.71 , pp. 19-39
    • Pomes, R.1    Roux, B.2
  • 19
    • 0015355244 scopus 로고
    • The plasma membranes of eye lens fibres. Biochemical and structural characterization
    • Bloemendal, H., Zweers, A., Vermorken, F., Dunia, I., and Benedetti, E. L. (1972) The plasma membranes of eye lens fibres. Biochemical and structural characterization. Cell Differ. 1, 91-106.
    • (1972) Cell Differ. , vol.1 , pp. 91-106
    • Bloemendal, H.1    Zweers, A.2    Vermorken, F.3    Dunia, I.4    Benedetti, E.L.5
  • 20
    • 0016775322 scopus 로고
    • Protein composition of bovine lens cortical fiber cell membranes
    • Alcala, J., Lieska, N., and Maisel, H. (1975) Protein composition of bovine lens cortical fiber cell membranes. Exp. Eye Res. 21, 581-595.
    • (1975) Exp. Eye Res. , vol.21 , pp. 581-595
    • Alcala, J.1    Lieska, N.2    Maisel, H.3
  • 21
    • 0020078925 scopus 로고
    • Immunocytochemical localization of the lens main intrinsic polypeptide (MIP26) in communicating junctions
    • Bok, D., Dockstader, J., and Horwitz, J. (1982) Immunocytochemical localization of the lens main intrinsic polypeptide (MIP26) in communicating junctions. J. Cell. Biol. 92, 213-220.
    • (1982) J. Cell. Biol. , vol.92 , pp. 213-220
    • Bok, D.1    Dockstader, J.2    Horwitz, J.3
  • 23
    • 0032546752 scopus 로고    scopus 로고
    • Purified lens major intrinsic protein (MIP) forms highly ordered tetragonal two-dimensional arrays by reconstitution
    • Hasler, L., Walz, T., Tittmann, P., Gross, H., Kistler, J., and Engel, A. (1998) Purified lens major intrinsic protein (MIP) forms highly ordered tetragonal two-dimensional arrays by reconstitution. J. Mol. Biol. 279, 855-864.
    • (1998) J. Mol. Biol. , vol.279 , pp. 855-864
    • Hasler, L.1    Walz, T.2    Tittmann, P.3    Gross, H.4    Kistler, J.5    Engel, A.6
  • 24
    • 0034698003 scopus 로고    scopus 로고
    • Surface tongue-and-groove contours on lens MIP facilitate cell-to-cell adherence
    • Fotiadis, D., Hasler, L., Müller, D. J., Stahlberg, H., Kistler, J., and Engel, A. (2000) Surface tongue-and-groove contours on lens MIP facilitate cell-to-cell adherence. J. Mol. Biol. 300, 779-789.
    • (2000) J. Mol. Biol. , vol.300 , pp. 779-789
    • Fotiadis, D.1    Hasler, L.2    Müller, D.J.3    Stahlberg, H.4    Kistler, J.5    Engel, A.6
  • 25
    • 4444382267 scopus 로고    scopus 로고
    • Aquaporin-0 membrane junctions form upon proteolytic cleavage
    • Gonen, T., Cheng, Y., Kistler, J., and Walz, T. (2004) Aquaporin-0 membrane junctions form upon proteolytic cleavage. J. Mol. Biol. 342, 1337-1345.
    • (2004) J. Mol. Biol. , vol.342 , pp. 1337-1345
    • Gonen, T.1    Cheng, Y.2    Kistler, J.3    Walz, T.4
  • 26
    • 3342946768 scopus 로고    scopus 로고
    • Post-translational modifications of aquaporin 0 (AQP0) in the normal human lens: Spatial and temporal occurrence
    • Ball, L. E., Garland, D. L., Crouch, R. K., and Schey, K. L. (2004) Post-translational modifications of aquaporin 0 (AQP0) in the normal human lens: spatial and temporal occurrence. Biochemistry 43, 9856-9865.
    • (2004) Biochemistry , vol.43 , pp. 9856-9865
    • Ball, L.E.1    Garland, D.L.2    Crouch, R.K.3    Schey, K.L.4
  • 27
    • 0027989801 scopus 로고
    • Molecular cloning of a mercurial-insensitive water channel expressed in selected water-transporting tissues
    • Hasegawa, H., Ma, T., Skach, W., Matthay, M. A., and Verkman, A. S. (1994) Molecular cloning of a mercurial-insensitive water channel expressed in selected water-transporting tissues. J. Biol. Chem. 269, 5497-5500.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5497-5500
    • Hasegawa, H.1    Ma, T.2    Skach, W.3    Matthay, M.A.4    Verkman, A.S.5
  • 28
    • 0028558703 scopus 로고
    • Molecular characterization of an aquaporin cDNA from brain: Candidate osmoreceptor and regulator of water balance
    • Jung, J. S., Bhat, R. V., Preston, G. M., Guggino, W. B., Baraban, J. M., and Agre, P. (1994) Molecular characterization of an aquaporin cDNA from brain: candidate osmoreceptor and regulator of water balance. Proc. Natl. Acad. Sci. USA. 91, 13052-13056.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 13052-13056
    • Jung, J.S.1    Bhat, R.V.2    Preston, G.M.3    Guggino, W.B.4    Baraban, J.M.5    Agre, P.6
  • 29
    • 0028175266 scopus 로고
    • Biologically active two-dimensional crystals of aquaporin CHIP
    • Walz, T., Smith, B. L., Zeidel, M. L., Engel, A., and Agre, P. (1994) Biologically active two-dimensional crystals of aquaporin CHIP. J. Biol. Chem. 269, 1583-1586.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1583-1586
    • Walz, T.1    Smith, B.L.2    Zeidel, M.L.3    Engel, A.4    Agre, P.5
  • 30
    • 28444442873 scopus 로고    scopus 로고
    • A census of ordered lipids and detergents in X-ray crystal structures of integral membrane proteins
    • Tamm, L. K., ed.. Wiley-VCH Verlag GmbH and Co., Weinheim
    • Wiener, M. (2005) A census of ordered lipids and detergents in X-ray crystal structures of integral membrane proteins. In Protein-Lipid Interactions: From Membrane Domains to Cellular Networks (Tamm, L. K., ed.). pp. 29-49, Wiley-VCH Verlag GmbH and Co., Weinheim.
    • (2005) Protein-Lipid Interactions: From Membrane Domains to Cellular Networks , pp. 29-49
    • Wiener, M.1
  • 32
    • 70349872605 scopus 로고    scopus 로고
    • Interactions of lipids with aquaporin-0 and other membrane proteins
    • in press
    • Hite, R. K., Gonen, T., Harrison, S. C., and Walz, T. Interactions of lipids with aquaporin-0 and other membrane proteins. Pflugers Arch in press.
    • Pflugers Arch
    • Hite, R.K.1    Gonen, T.2    Harrison, S.C.3    Walz, T.4


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