메뉴 건너뛰기




Volumn 47, Issue 4, 2006, Pages 1562-1570

The C terminus of lens aquaporin 0 interacts with the cytoskeletal proteins filensin and CP49

Author keywords

[No Author keywords available]

Indexed keywords

AQUAPORIN; AQUAPORIN 0; CYTOSKELETON PROTEIN; FILENSIN; LENS PROTEIN; PROTEIN CP49; UNCLASSIFIED DRUG; EYE PROTEIN; INTERMEDIATE FILAMENT PROTEIN; MEMBRANE PROTEIN; PEPTIDE FRAGMENT; PHAKININ;

EID: 33646000308     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: 10.1167/iovs.05-1313     Document Type: Article
Times cited : (87)

References (49)
  • 1
    • 0028326794 scopus 로고
    • Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine
    • Deen PM, Verdijk MA, Knoers NV, et al. Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine. Science. 1994;264:92-95.
    • (1994) Science , vol.264 , pp. 92-95
    • Deen, P.M.1    Verdijk, M.A.2    Knoers, N.V.3
  • 2
    • 0034703396 scopus 로고    scopus 로고
    • Functional impairment of lens aquaporin in two families with dominantly inherited cataracts
    • Francis P, Chung JJ, Yasui M, et al. Functional impairment of lens aquaporin in two families with dominantly inherited cataracts. Hum Mol Genet. 2000;9:2329-2334.
    • (2000) Hum Mol Genet , vol.9 , pp. 2329-2334
    • Francis, P.1    Chung, J.J.2    Yasui, M.3
  • 3
    • 0029910115 scopus 로고    scopus 로고
    • Phylogenetic characterization of the mip family of transmembrane channel proteins
    • Park JH, Saier MH Jr. Phylogenetic characterization of the mip family of transmembrane channel proteins. J Membr Biol. 1996;153:171-180.
    • (1996) J Membr Biol , vol.153 , pp. 171-180
    • Park, J.H.1    Saier Jr., M.H.2
  • 5
    • 0018081108 scopus 로고
    • Immunofluorescent study of a chick lens fiber cell membrane polypeptide
    • Waggoner PR, Maisel H. Immunofluorescent study of a chick lens fiber cell membrane polypeptide. Exp Eye Res. 1978;27:151-157.
    • (1978) Exp Eye Res , vol.27 , pp. 151-157
    • Waggoner, P.R.1    Maisel, H.2
  • 7
    • 0036829071 scopus 로고    scopus 로고
    • The role of putative phosphorylation sites in the targeting and shuttling of the aquaporin-2 water channel
    • van Balkom BW, Savelkoul PJ, Markovich D, et al. The role of putative phosphorylation sites in the targeting and shuttling of the aquaporin-2 water channel. J Biol Chem. 2002;277:41473-41479.
    • (2002) J Biol Chem , vol.277 , pp. 41473-41479
    • van Balkom, B.W.1    Savelkoul, P.J.2    Markovich, D.3
  • 8
    • 0036314938 scopus 로고    scopus 로고
    • Identification and structure of a putative ca2+-binding domain at the c terminus of aqp1
    • Fotiadis D, Suda K, Tittmann P, et al. Identification and structure of a putative ca2+-binding domain at the c terminus of aqp1. J Mol Biol. 2002;318:1381-1394.
    • (2002) J Mol Biol , vol.318 , pp. 1381-1394
    • Fotiadis, D.1    Suda, K.2    Tittmann, P.3
  • 10
    • 0034711225 scopus 로고    scopus 로고
    • Regulation of aquaporin-2 trafficking by vasopressin in the renal collecting duct. Roles of ryanodine-sensitive ca2+ stores and calmodulin
    • Chou CL, Yip KP, Michea L, et al. Regulation of aquaporin-2 trafficking by vasopressin in the renal collecting duct. Roles of ryanodine-sensitive ca2+ stores and calmodulin. J Biol Chem. 2000;275:36839-36846.
    • (2000) J Biol Chem , vol.275 , pp. 36839-36846
    • Chou, C.L.1    Yip, K.P.2    Michea, L.3
  • 11
    • 0041721625 scopus 로고    scopus 로고
    • Ph and calcium regulate the water permeability of aquaporin 0
    • Nemeth-Cahalan KL, Hall JE. Ph and calcium regulate the water permeability of aquaporin 0. J Biol Chem. 2000;275:6777-6782.
    • (2000) J Biol Chem , vol.275 , pp. 6777-6782
    • Nemeth-Cahalan, K.L.1    Hall, J.E.2
  • 13
    • 0025826151 scopus 로고
    • Calmodulin interacts with a c-terminus peptide from the lens membrane protein mip26
    • Girsch SJ, Peracchia C. Calmodulin interacts with a c-terminus peptide from the lens membrane protein mip26. Curr Eye Res. 1991;10:839-849.
    • (1991) Curr Eye Res , vol.10 , pp. 839-849
    • Girsch, S.J.1    Peracchia, C.2
  • 14
    • 20444505236 scopus 로고    scopus 로고
    • Developmental regulation of the direct interaction between the intracellular loop of connexin 45.6 and the c terminus of major intrinsic protein (aquaporin-0)
    • Yu XS, Yin X, Lafer EM, Jiang JX. Developmental regulation of the direct interaction between the intracellular loop of connexin 45.6 and the c terminus of major intrinsic protein (aquaporin-0). J Biol Chem. 2005;280:22081-22090.
    • (2005) J Biol Chem , vol.280 , pp. 22081-22090
    • Yu, X.S.1    Yin, X.2    Lafer, E.M.3    Jiang, J.X.4
  • 15
    • 25444473974 scopus 로고    scopus 로고
    • Specific interaction between lens mip/aquaporin-0 and two members of the gamma-crystallin family
    • Fan J, Fariss RN, Purkiss AG, et al. Specific interaction between lens mip/aquaporin-0 and two members of the gamma-crystallin family. Mol Vis. 2005;11:76-87.
    • (2005) Mol Vis , vol.11 , pp. 76-87
    • Fan, J.1    Fariss, R.N.2    Purkiss, A.G.3
  • 16
    • 0019194787 scopus 로고
    • The surface morphology of embryonic and adult chick lens-fiber cells
    • Kuszak J, Alcala J, Maisel H. The surface morphology of embryonic and adult chick lens-fiber cells. Am J Anat. 1980;159:395-410.
    • (1980) Am J Anat , vol.159 , pp. 395-410
    • Kuszak, J.1    Alcala, J.2    Maisel, H.3
  • 17
    • 0029874569 scopus 로고    scopus 로고
    • Electron microscopic observations of the crystalline lens
    • Kuszak JR, Peterson KL, Brown HG. Electron microscopic observations of the crystalline lens. Microsc Res Tech. 1996;33:441-479.
    • (1996) Microsc Res Tech , vol.33 , pp. 441-479
    • Kuszak, J.R.1    Peterson, K.L.2    Brown, H.G.3
  • 18
    • 0033776421 scopus 로고    scopus 로고
    • Epithelial organization of the mammalian lens
    • Zampighi GA, Eskandari S, Kreman M. Epithelial organization of the mammalian lens. Exp Eye Res. 2000;71:415-435.
    • (2000) Exp Eye Res , vol.71 , pp. 415-435
    • Zampighi, G.A.1    Eskandari, S.2    Kreman, M.3
  • 19
    • 0023424908 scopus 로고
    • Electron microscopic observations of reconstituted proteoliposomes with the purified major intrinsic membrane protein of eye lens fibers
    • Dunia I, Manenti S, Rousselet A, Benedetti EL. Electron microscopic observations of reconstituted proteoliposomes with the purified major intrinsic membrane protein of eye lens fibers. J Cell Biol. 1987;105:1679-1689.
    • (1987) J Cell Biol , vol.105 , pp. 1679-1689
    • Dunia, I.1    Manenti, S.2    Rousselet, A.3    Benedetti, E.L.4
  • 22
    • 0033729222 scopus 로고    scopus 로고
    • Disruption of lens fiber cell architecture in mice expressing a chimeric aqp0-ltr protein
    • Shiels A, Mackay D, Bassnett S, Al-Ghoul K, Kuszak J. Disruption of lens fiber cell architecture in mice expressing a chimeric aqp0-ltr protein. FASEB J. 2000;14:2207-2212.
    • (2000) FASEB J , vol.14 , pp. 2207-2212
    • Shiels, A.1    Mackay, D.2    Bassnett, S.3    Al-Ghoul, K.4    Kuszak, J.5
  • 23
    • 3342946768 scopus 로고    scopus 로고
    • Post-translational modifications of aquaporin 0 (aqp0) in the normal human lens: Spatial and temporal occurrence
    • Ball LE, Garland DL, Crouch RK, Schey KL. Post-translational modifications of aquaporin 0 (aqp0) in the normal human lens: Spatial and temporal occurrence. Biochemistry. 2004;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
  • 25
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng JK, McCormack AL, Yates III JR. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom. 1994;5:976-989.
    • (1994) J Am Soc Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 26
    • 0023399896 scopus 로고
    • Characterization by tandem mass spectrometry of structural modifications in proteins
    • Biemann K, Scoble HA. Characterization by tandem mass spectrometry of structural modifications in proteins. Science. 1987;237:992-998.
    • (1987) Science , vol.237 , pp. 992-998
    • Biemann, K.1    Scoble, H.A.2
  • 27
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by ms/ms and database search
    • Keller A, Nesvizhskii AI, Kolker E, Aebersold R. Empirical statistical model to estimate the accuracy of peptide identifications made by ms/ms and database search. Anal Chem. 2002;74:5383-5392.
    • (2002) Anal Chem , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 28
    • 14244266211 scopus 로고    scopus 로고
    • The intermediate filament systems in the eye lens
    • Perng MD, Sandilands A, Kuszak J, et al. The intermediate filament systems in the eye lens. Methods Cell Biol. 2004;78:597-624.
    • (2004) Methods Cell Biol , vol.78 , pp. 597-624
    • Perng, M.D.1    Sandilands, A.2    Kuszak, J.3
  • 29
    • 0028831015 scopus 로고
    • In vitro studies on the assembly properties of the lens proteins cp49, cp115: Coassembly with alpha-crystallin but not with vimentin
    • Carter JM, Hutcheson AM, Quinlan RA. In vitro studies on the assembly properties of the lens proteins cp49, cp115: coassembly with alpha-crystallin but not with vimentin. Exp Eye Res. 1995;60:181-192.
    • (1995) Exp Eye Res , vol.60 , pp. 181-192
    • Carter, J.M.1    Hutcheson, A.M.2    Quinlan, R.A.3
  • 30
    • 0345550308 scopus 로고    scopus 로고
    • Bfsp2 mutation found in mouse 129 strains causes the loss of cp49′ and induces vimentin-dependent changes in the lens fibre cell cytoskeleton
    • Sandilands A, Wang X, Hutcheson AM, et al. Bfsp2 mutation found in mouse 129 strains causes the loss of cp49′ and induces vimentin-dependent changes in the lens fibre cell cytoskeleton. Exp Eye Res. 2004;78:875-889.
    • (2004) Exp Eye Res , vol.78 , pp. 875-889
    • Sandilands, A.1    Wang, X.2    Hutcheson, A.M.3
  • 31
    • 0028905818 scopus 로고
    • Vimentin and cp49/filensin form distinct networks in the lens which are independently modulated during lens fibre cell differentiation
    • Sandilands A, Prescott AR, Carter JM, et al. Vimentin and cp49/filensin form distinct networks in the lens which are independently modulated during lens fibre cell differentiation. J Cell Sci. 1995;108(Pt 4):1397-1406.
    • (1995) J Cell Sci , vol.108 , Issue.PART 4 , pp. 1397-1406
    • Sandilands, A.1    Prescott, A.R.2    Carter, J.M.3
  • 33
    • 0024166479 scopus 로고
    • Immunochemical characterization of a mr 115 lens fiber cell-specific extrinsic membrane protein
    • FitzGerald PG. Immunochemical characterization of a mr 115 lens fiber cell-specific extrinsic membrane protein. Curr Eye Res. 1988;7:1243-1253.
    • (1988) Curr Eye Res , vol.7 , pp. 1243-1253
    • FitzGerald, P.G.1
  • 34
    • 0026706184 scopus 로고
    • Cdna sequence analysis of cp94: Rat lens fiber cell beaded-filament structural protein shows homology to cytokeratins
    • Masaki S, Watanabe T. Cdna sequence analysis of cp94: rat lens fiber cell beaded-filament structural protein shows homology to cytokeratins. Biochem Biophys Res Commun. 1992;186:190-198.
    • (1992) Biochem Biophys Res Commun , vol.186 , pp. 190-198
    • Masaki, S.1    Watanabe, T.2
  • 35
    • 0027180063 scopus 로고
    • Evidence that the chick lens cytoskeletal protein cp 49 belongs to the family of intermediate filament proteins
    • Orii H, Agata K, Sawada K, Eguchi G, Maisel H. Evidence that the chick lens cytoskeletal protein cp 49 belongs to the family of intermediate filament proteins. Curr Eye Res. 1993;12:583-588.
    • (1993) Curr Eye Res , vol.12 , pp. 583-588
    • Orii, H.1    Agata, K.2    Sawada, K.3    Eguchi, G.4    Maisel, H.5
  • 36
    • 0027449959 scopus 로고
    • Dynamics of intermediate filaments: Recent progress and unanswered questions
    • Georgatos SD. Dynamics of intermediate filaments: recent progress and unanswered questions. FEBS Lett. 1993;318:101-107.
    • (1993) FEBS Lett , vol.318 , pp. 101-107
    • Georgatos, S.D.1
  • 37
    • 0027153962 scopus 로고
    • Bovine filensin possesses primary and secondary structure similarity to intermediate filament proteins
    • Gounari F, Merdes A, Quinlan R, et al. Bovine filensin possesses primary and secondary structure similarity to intermediate filament proteins. J Cell Biol. 1993;121:847-853.
    • (1993) J Cell Biol , vol.121 , pp. 847-853
    • Gounari, F.1    Merdes, A.2    Quinlan, R.3
  • 38
    • 0027722988 scopus 로고
    • The 47-kd lens-specific protein phakinin is a tailless intermediate filament protein and an assembly partner of filensin
    • Merdes A, Gounari F, Georgatos SD. The 47-kd lens-specific protein phakinin is a tailless intermediate filament protein and an assembly partner of filensin. J Cell Biol. 1993;123:1507-1516.
    • (1993) J Cell Biol , vol.123 , pp. 1507-1516
    • Merdes, A.1    Gounari, F.2    Georgatos, S.D.3
  • 39
    • 0029911721 scopus 로고    scopus 로고
    • Gene structure and cdna sequence identify the beaded filament protein cp49 as a highly divergent type i intermediate filament protein
    • Hess JF, Casselman JT, FitzGerald PG. Gene structure and cdna sequence identify the beaded filament protein cp49 as a highly divergent type i intermediate filament protein. J Biol Chem. 1996;271:6729-6735.
    • (1996) J Biol Chem , vol.271 , pp. 6729-6735
    • Hess, J.F.1    Casselman, J.T.2    FitzGerald, P.G.3
  • 40
    • 0030693791 scopus 로고    scopus 로고
    • Gene structure and sequence comparisons of the eye lens specific protein, filensin, from rat and mouse: Implications for protein classification and assembly
    • Masaki S, Quinlan RA. Gene structure and sequence comparisons of the eye lens specific protein, filensin, from rat and mouse: Implications for protein classification and assembly. Gene. 1997;201:11-20.
    • (1997) Gene , vol.201 , pp. 11-20
    • Masaki, S.1    Quinlan, R.A.2
  • 41
    • 0032077115 scopus 로고    scopus 로고
    • Primary sequence, secondary structure, gene structure, and assembly properties suggests that the lens-specific cytoskeletal protein filensin represents a novel class of intermediate filament protein
    • Hess JF, Casselman JT, Kong AP, FitzGerald PG. Primary sequence, secondary structure, gene structure, and assembly properties suggests that the lens-specific cytoskeletal protein filensin represents a novel class of intermediate filament protein. Exp Eye Res. 1998;66:625-644.
    • (1998) Exp Eye Res , vol.66 , pp. 625-644
    • Hess, J.F.1    Casselman, J.T.2    Kong, A.P.3    FitzGerald, P.G.4
  • 42
    • 0021215563 scopus 로고
    • A cytoskeletal protein unique to lens fiber cell differentiation
    • Ireland M, Maisel H. A cytoskeletal protein unique to lens fiber cell differentiation. Exp Eye Res. 1984;38:637-645.
    • (1984) Exp Eye Res , vol.38 , pp. 637-645
    • Ireland, M.1    Maisel, H.2
  • 43
    • 0024474174 scopus 로고
    • The mr 115 kd fiber cell-specific protein is a component of the lens cytoskeleton
    • FitzGerald PG, Gottlieb W. The mr 115 kd fiber cell-specific protein is a component of the lens cytoskeleton. Curr Eye Res. 1989;8:801-811.
    • (1989) Curr Eye Res , vol.8 , pp. 801-811
    • FitzGerald, P.G.1    Gottlieb, W.2
  • 44
    • 0024210122 scopus 로고
    • Age-related changes in a fiber cell-specific extrinsic membrane protein
    • FitzGerald PG. Age-related changes in a fiber cell-specific extrinsic membrane protein. Curr Eye Res. 1988;7:1255-1262.
    • (1988) Curr Eye Res , vol.7 , pp. 1255-1262
    • FitzGerald, P.G.1
  • 45
    • 0026046947 scopus 로고
    • Filensin: A new vimentin-binding, polymerization-competent, and membrane-associated protein of the lens fiber cell
    • Merdes A, Brunkener M, Horstmann H, Georgatos SD. Filensin: a new vimentin-binding, polymerization-competent, and membrane-associated protein of the lens fiber cell. J Cell Biol. 1991;115:397-410.
    • (1991) J Cell Biol , vol.115 , pp. 397-410
    • Merdes, A.1    Brunkener, M.2    Horstmann, H.3    Georgatos, S.D.4
  • 46
    • 19044392016 scopus 로고    scopus 로고
    • Optical dysfunction of the crystalline lens in aquaporin-0-deficient mice
    • Shiels A, Bassnett S, Varadaraj K, et al. Optical dysfunction of the crystalline lens in aquaporin-0-deficient mice. Physiol Genomics. 2001;7:179-186.
    • (2001) Physiol Genomics , vol.7 , pp. 179-186
    • Shiels, A.1    Bassnett, S.2    Varadaraj, K.3
  • 48
    • 0036902453 scopus 로고    scopus 로고
    • Targeted genomic deletion of the lens-specific intermediate filament protein cp49
    • Alizadeh A, Clark JI, Seeberger T, et al. Targeted genomic deletion of the lens-specific intermediate filament protein cp49. Invest Ophthalmol Vis Sci. 2002;43:3722-3727.
    • (2002) Invest Ophthalmol Vis Sci , vol.43 , pp. 3722-3727
    • Alizadeh, A.1    Clark, J.I.2    Seeberger, T.3
  • 49
    • 0037373876 scopus 로고    scopus 로고
    • Knockout of the intermediate filament protein cp49 destabilises the lens fibre cell cytoskeleton and decreases lens optical quality, but does not induce cataract
    • Sandilands A, Prescott AR, Wegener A, et al. Knockout of the intermediate filament protein cp49 destabilises the lens fibre cell cytoskeleton and decreases lens optical quality, but does not induce cataract. Exp Eye Res. 2003;76:385-391.
    • (2003) Exp Eye Res , vol.76 , pp. 385-391
    • Sandilands, A.1    Prescott, A.R.2    Wegener, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.