메뉴 건너뛰기




Volumn 128, Issue 3, 1999, Pages 287-296

Oligomerization state of MIP proteins expressed in Xenopus oocytes as revealed by freeze-fracture electron-microscopy analysis

Author keywords

Electron microscopy; Freeze fracture; MIP family; Oligomerization state; Orthogonal array; Xenopus oocyte

Indexed keywords

AQUAPORIN; CARRIER PROTEIN; COMPLEMENTARY RNA; MEMBRANE PROTEIN;

EID: 0033619938     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1999.4196     Document Type: Article
Times cited : (28)

References (46)
  • 1
    • 0025333990 scopus 로고
    • Hydrodynamic characterization of the major intrinsic protein from the bovine lens fiber membranes
    • Aerst T., Xia J. Z., Slegers H., De Block J., Clauwaert J. Hydrodynamic characterization of the major intrinsic protein from the bovine lens fiber membranes. J. Biol. Chem. 265:1990;8675-8680.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8675-8680
    • Aerst, T.1    Xia, J.Z.2    Slegers, H.3    De Block, J.4    Clauwaert, J.5
  • 3
    • 0020792595 scopus 로고
    • Freeze-fracture electron microscopy of membranes changes in progesterone-induced oocytes and eggs of Xenopus laevis
    • Bluemink J. G., Hage W. J., Van Den Hoef M. H. F., Dictus W. J. A. G. Freeze-fracture electron microscopy of membranes changes in progesterone-induced oocytes and eggs of Xenopus laevis. Eur. J. Cell. Biol. 31:1983;85-93.
    • (1983) Eur. J. Cell. Biol. , vol.31 , pp. 85-93
    • Bluemink, J.G.1    Hage, W.J.2    Van Den Hoef, M.H.F.3    Dictus, W.J.A.G.4
  • 5
    • 0016283085 scopus 로고
    • Membrane associated particles: Distribution in frog urinary bladder epithelium at rest and after oxytocin treatment
    • Chevalier J., Bourguet J., Hugon J. S. Membrane associated particles: Distribution in frog urinary bladder epithelium at rest and after oxytocin treatment. Cell Tissue Res. 152:1974;129-140.
    • (1974) Cell Tissue Res. , vol.152 , pp. 129-140
    • Chevalier, J.1    Bourguet, J.2    Hugon, J.S.3
  • 6
    • 0018710386 scopus 로고
    • Particle aggregates during antidiuretic action. Some comments on their formation
    • Chevalier J., Parisi M., Bourget J. Particle aggregates during antidiuretic action. Some comments on their formation. Biol. Cell. 35:1979;207-210.
    • (1979) Biol. Cell. , vol.35 , pp. 207-210
    • Chevalier, J.1    Parisi, M.2    Bourget, J.3
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project 4
    • Collaborative Computational Project 4. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. Sect. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 760-763
  • 9
    • 0028020911 scopus 로고
    • Cloning and expression of AQP3, a water channel from the medullary collecting duct of rat kidney
    • Echevarria M., Windhager E. E., Tate S. S., Frindt G. Cloning and expression of AQP3, a water channel from the medullary collecting duct of rat kidney. Proc. Natl. Acad. Sci. USA. 91:1994;10997-11001.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10997-11001
    • Echevarria, M.1    Windhager, E.E.2    Tate, S.S.3    Frindt, G.4
  • 10
    • 0025120896 scopus 로고
    • Properties of channels reconstituted from the major intrinsic protein of lens fiber membranes
    • Ehring G. R., Zampighi G., Horwitz J., Bok D., Hall J. E. Properties of channels reconstituted from the major intrinsic protein of lens fiber membranes. J. Gen. Physiol. 96:1990;631-664.
    • (1990) J. Gen. Physiol. , vol.96 , pp. 631-664
    • Ehring, G.R.1    Zampighi, G.2    Horwitz, J.3    Bok, D.4    Hall, J.E.5
  • 11
    • 0032530592 scopus 로고    scopus 로고
    • Structural analysis of cloned plasma membrane proteins by freeze-fracture electron microscopy
    • Eskandari S., Wright E. M., Kreman M., Starace D. M., Zampighi G. A. Structural analysis of cloned plasma membrane proteins by freeze-fracture electron microscopy. Proc. Natl. Acad. Sci. USA. 95:1998;11235-11240.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11235-11240
    • Eskandari, S.1    Wright, E.M.2    Kreman, M.3    Starace, D.M.4    Zampighi, G.A.5
  • 12
    • 0019707963 scopus 로고
    • SPIDER - A modular software system for electron image processing
    • Frank J., Shimkin B., Dowse H. SPIDER - A modular software system for electron image processing. Ultramicroscopy. 6:1981;343-358.
    • (1981) Ultramicroscopy , vol.6 , pp. 343-358
    • Frank, J.1    Shimkin, B.2    Dowse, H.3
  • 13
    • 0024387482 scopus 로고
    • Structural and biochemical observations on specialized membranes of the "filter chamber," a water-shunting complex in sap-sucking homopteran insects
    • Hubert J. F., Thomas D., Cavalier A., Gouranton J. Structural and biochemical observations on specialized membranes of the "filter chamber," a water-shunting complex in sap-sucking homopteran insects. Biol. Cell. 66:1989;155-163.
    • (1989) Biol. Cell , vol.66 , pp. 155-163
    • Hubert, J.F.1    Thomas, D.2    Cavalier, A.3    Gouranton, J.4
  • 14
    • 0030860531 scopus 로고    scopus 로고
    • Cloning and functional expression of a new water channel abundantly expressed in the testis permeable to water, glycerol, and urea
    • Ishibashi K., Kuwahara M., Gu Y., Kageyama Y., Tohsaka A., Suzuki F., Marumo F., Sasaki S. Cloning and functional expression of a new water channel abundantly expressed in the testis permeable to water, glycerol, and urea. J. Biol. Chem. 272:1997;20782-20786.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20782-20786
    • Ishibashi, K.1    Kuwahara, M.2    Gu, Y.3    Kageyama, Y.4    Tohsaka, A.5    Suzuki, F.6    Marumo, F.7    Sasaki, S.8
  • 15
    • 22044457833 scopus 로고    scopus 로고
    • The dichotomy of MIP family suggests two separate origins of water channels
    • Ishibashi K., Sasaki S. The dichotomy of MIP family suggests two separate origins of water channels. News Physiol. Sci. 13:1998;137-142.
    • (1998) News Physiol. Sci. , vol.13 , pp. 137-142
    • Ishibashi, K.1    Sasaki, S.2
  • 16
    • 0028227129 scopus 로고
    • Molecular cloning and expression of a member of the aquaporin family with permeability to glycerol and urea in addition to water expressed at the basolateral membrane of kidney collecting duct cells
    • Ishibashi K., Sasaki S., Fushimi K., Uchida S., Kuwahara M., Saito H., Furakawa T., Nakajima K., Yamaguchi Y., Gojobori T., Marumo F. Molecular cloning and expression of a member of the aquaporin family with permeability to glycerol and urea in addition to water expressed at the basolateral membrane of kidney collecting duct cells. Proc. Natl. Acad. Sci. USA. 91:1994;6269-6273.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6269-6273
    • Ishibashi, K.1    Sasaki, S.2    Fushimi, K.3    Uchida, S.4    Kuwahara, M.5    Saito, H.6    Furakawa, T.7    Nakajima, K.8    Yamaguchi, Y.9    Gojobori, T.10    Marumo, F.11
  • 17
    • 0028318868 scopus 로고
    • Molecular structure of the water channel through aquaporin CHIP
    • Jung J. S., Preston G. M., Smith B. L., Guggino W. B., Agre P. Molecular structure of the water channel through aquaporin CHIP. J. Biol. Chem. 269:1994;14648-14654.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14648-14654
    • Jung, J.S.1    Preston, G.M.2    Smith, B.L.3    Guggino, W.B.4    Agre, P.5
  • 18
    • 0016823860 scopus 로고
    • Vasopresin: Induced structural change in toad bladder luminal membrane
    • Kachadorian W. A., Wade J. B., Discala V. A. Vasopresin: Induced structural change in toad bladder luminal membrane. Science. 190:1975;67-69.
    • (1975) Science , vol.190 , pp. 67-69
    • Kachadorian, W.A.1    Wade, J.B.2    Discala, V.A.3
  • 19
    • 0033522389 scopus 로고    scopus 로고
    • An impaired routing of wild-type aquaporin-2 after tetramerization with an aquaporin-2 mutant explains dominant nephrogenic diabetes insipidus
    • Kamsteeg E. J., Wormhoudt T. A., Rijss J. P., Van Os C. H., Deen P. M. An impaired routing of wild-type aquaporin-2 after tetramerization with an aquaporin-2 mutant explains dominant nephrogenic diabetes insipidus. EMBO J. 18:1999;2394-2400.
    • (1999) EMBO J. , vol.18 , pp. 2394-2400
    • Kamsteeg, E.J.1    Wormhoudt, T.A.2    Rijss, J.P.3    Van Os, C.H.4    Deen, P.M.5
  • 20
    • 0031556944 scopus 로고    scopus 로고
    • Characterisation of the major intrinsic protein (MIP) from bovine lens fiber membranes by electron microscopy and hydrodynamics
    • König N., Zampighi G. A., Butler P. J. Characterisation of the major intrinsic protein (MIP) from bovine lens fiber membranes by electron microscopy and hydrodynamics. J. Mol. Biol. 265:1997;590-602.
    • (1997) J. Mol. Biol. , vol.265 , pp. 590-602
    • König, N.1    Zampighi, G.A.2    Butler, P.J.3
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0032524648 scopus 로고    scopus 로고
    • A yeast recombinant aquaporin mutant that is not expressed or mistargeted in Xenopus oocyte can be functionally analyzed in reconstituted proteoliposomes
    • Lagrée V., Pellerin I., Hubert J. F., Tacnet F., Le Cahérec F., Roudier N., Thomas D., Gouranton J., Deschamps S. A yeast recombinant aquaporin mutant that is not expressed or mistargeted in Xenopus oocyte can be functionally analyzed in reconstituted proteoliposomes. J. Biol. Chem. 273:1998a;12422-12426.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12422-12426
    • Lagrée, V.1    Pellerin, I.2    Hubert, J.F.3    Tacnet, F.4    Le Cahérec, F.5    Roudier, N.6    Thomas, D.7    Gouranton, J.8    Deschamps, S.9
  • 28
    • 0030915303 scopus 로고    scopus 로고
    • Molecular design of aquaporin-1 water channel as revealed by electron crystallography
    • Li H., Lee S., Jap B. K. Molecular design of aquaporin-1 water channel as revealed by electron crystallography. Nat. Struct. Biol. 4:1997;263-265.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 263-265
    • Li, H.1    Lee, S.2    Jap, B.K.3
  • 29
    • 0028059494 scopus 로고
    • Cloning of a water channel homolog expressed in brain meningeal cells and kidney collecting duct that functions as a stilbene-sensitive glycerol transporter
    • Ma T., Frigeri A., Hasegawa H., Verkman A. S. Cloning of a water channel homolog expressed in brain meningeal cells and kidney collecting duct that functions as a stilbene-sensitive glycerol transporter. J. Biol. Chem. 269:1994;21845-21849.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21845-21849
    • Ma, T.1    Frigeri, A.2    Hasegawa, H.3    Verkman, A.S.4
  • 31
    • 0026503030 scopus 로고
    • Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein
    • Preston G. M., Carroll T. P., Guggino W. B., Agre P. Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science. 256:1992;385-387.
    • (1992) Science , vol.256 , pp. 385-387
    • Preston, G.M.1    Carroll, T.P.2    Guggino, W.B.3    Agre, P.4
  • 32
    • 0342847085 scopus 로고    scopus 로고
    • Two-dimensional crystals of a procaryotic water channel: AqpZ from Escherichia coli
    • Ringler P., Borgnia M., Scheuring S., Agre P., Engel A. Two-dimensional crystals of a procaryotic water channel: AqpZ from Escherichia coli. Biol. Cell. 90:1998;33-34.
    • (1998) Biol. Cell. , vol.90 , pp. 33-34
    • Ringler, P.1    Borgnia, M.2    Scheuring, S.3    Agre, P.4    Engel, A.5
  • 33
    • 0030665695 scopus 로고    scopus 로고
    • MACS: Automatic counting of objects based on shape recognition
    • Rolland J. P., Bron P., Thomas D. MACS: Automatic counting of objects based on shape recognition. Comput. Appl. Biosci. 13:1997;563-564.
    • (1997) Comput. Appl. Biosci. , vol.13 , pp. 563-564
    • Rolland, J.P.1    Bron, P.2    Thomas, D.3
  • 35
    • 0025078661 scopus 로고
    • Use of Xenopus oocytes for the functional expression of plasma membrane proteins
    • Sigel E. Use of Xenopus oocytes for the functional expression of plasma membrane proteins. J. Membr. Biol. 117:1990;201-221.
    • (1990) J. Membr. Biol. , vol.117 , pp. 201-221
    • Sigel, E.1
  • 36
    • 0025922827 scopus 로고
    • r 28 000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins
    • r 28 000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins. J. Biol. Chem. 266:1991;6407-6415.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6407-6415
    • Smith, B.L.1    Agre, P.2
  • 38
    • 0031668235 scopus 로고    scopus 로고
    • Freeze-fracture analysis of plasma membranes of CHO cells stably expressing aquaporins 1-5
    • Van Hoek A. N., Yang B., Kirmiz S., Brown D. Freeze-fracture analysis of plasma membranes of CHO cells stably expressing aquaporins 1-5. J. Membr. Biol. 165:1998;243-254.
    • (1998) J. Membr. Biol. , vol.165 , pp. 243-254
    • Van Hoek, A.N.1    Yang, B.2    Kirmiz, S.3    Brown, D.4
  • 41
    • 0030775672 scopus 로고    scopus 로고
    • Absence of orthogonal arrays in kidney, brain and muscle from transgenic knockout mice lacking water channel aquaporin-4
    • Verbavatz J. M., Ma T., Gobin R., Verkman A. S. Absence of orthogonal arrays in kidney, brain and muscle from transgenic knockout mice lacking water channel aquaporin-4. J. Cell Sci. 110:1997;2855-2860.
    • (1997) J. Cell Sci. , vol.110 , pp. 2855-2860
    • Verbavatz, J.M.1    Ma, T.2    Gobin, R.3    Verkman, A.S.4
  • 44
    • 0029375244 scopus 로고
    • Projection map of aquaporin-1 determined by electron crystallography
    • Walz T., Typke D., Smith B. L., Agre P., Engel A. Projection map of aquaporin-1 determined by electron crystallography. Nat. Struct. Biol. 2:1995;730-732.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 730-732
    • Walz, T.1    Typke, D.2    Smith, B.L.3    Agre, P.4    Engel, A.5
  • 45
    • 0029926097 scopus 로고    scopus 로고
    • The mercurial insensitive water channel (AQP-4) forms orthogonal arrays in stably transfected Chinese hamster ovary cells
    • Yang B., Brown D., Verkman A. S. The mercurial insensitive water channel (AQP-4) forms orthogonal arrays in stably transfected Chinese hamster ovary cells. J. Biol. Chem. 271:1996;4577-4580.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4577-4580
    • Yang, B.1    Brown, D.2    Verkman, A.S.3
  • 46
    • 0028806397 scopus 로고
    • A method for determining the unitary functional capacity of cloned channels and transporters expressed in Xenopus laevis oocytes
    • Zampighi G. A., Kreman M., Boorer K. J., Loo D. D. F., Benazilla F., Chandy G., Hall J. E., Wright E. M. A method for determining the unitary functional capacity of cloned channels and transporters expressed in Xenopus laevis oocytes. J. Membr. Biol. 148:1995;65-78.
    • (1995) J. Membr. Biol. , vol.148 , pp. 65-78
    • Zampighi, G.A.1    Kreman, M.2    Boorer, K.J.3    Loo, D.D.F.4    Benazilla, F.5    Chandy, G.6    Hall, J.E.7    Wright, E.M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.