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Volumn 308, Issue 6, 2015, Pages L569-L576

Alcohol-induced ciliary dysfunction targets the outer dynein arm

Author keywords

Alcohol; Cilia; Dynein; Ethanol

Indexed keywords

ALCOHOL; DYNEIN ADENOSINE TRIPHOSPHATASE; PHOSPHOPROTEIN; CENTRAL DEPRESSANT AGENT;

EID: 84937696040     PISSN: 10400605     EISSN: 15221504     Source Type: Journal    
DOI: 10.1152/ajplung.00257.2014     Document Type: Article
Times cited : (17)

References (54)
  • 1
    • 7944223873 scopus 로고    scopus 로고
    • Cilia-related diseases
    • Afzelius BA. Cilia-related diseases. J Pathol 204: 470-477, 2004.
    • (2004) J Pathol , vol.204 , pp. 470-477
    • Afzelius, B.A.1
  • 2
    • 67650469447 scopus 로고    scopus 로고
    • Analysis of flagellar phosphoproteins from Chlamydomonas reinhardtii
    • Boesger J, Wagner V, Weisheit W, Mittag M. Analysis of flagellar phosphoproteins from Chlamydomonas reinhardtii. Eukaryot Cell 8: 922- 932, 2009.
    • (2009) Eukaryot Cell , vol.8 , pp. 922-932
    • Boesger, J.1    Wagner, V.2    Weisheit, W.3    Mittag, M.4
  • 3
    • 84876552918 scopus 로고    scopus 로고
    • The N-DRC forms a conserved biochemical complex that maintains outer doublet alignment and limits microtubule sliding in motile axonemes
    • Bower R, Tritschler D, Vanderwaal K, Perrone CA, Mueller J, Fox L, Sale WS, Porter ME. The N-DRC forms a conserved biochemical complex that maintains outer doublet alignment and limits microtubule sliding in motile axonemes. Mol Biol Cell 24: 1134-1152, 2013.
    • (2013) Mol Biol Cell , vol.24 , pp. 1134-1152
    • Bower, R.1    Tritschler, D.2    Vanderwaal, K.3    Perrone, C.A.4    Mueller, J.5    Fox, L.6    Sale, W.S.7    Porter, M.E.8
  • 4
    • 0141632803 scopus 로고    scopus 로고
    • DC3, the 21-kDa subunit of the outer dynein arm-docking complex (ODA-DC), is a novel EF-hand protein important for assembly of both the outer arm and the ODA-DC
    • Casey DM, Inaba K, Pazour GJ, Takada S, Wakabayashi K, Wilkerson CG, Kamiya R, Witman GB. DC3, the 21-kDa subunit of the outer dynein arm-docking complex (ODA-DC), is a novel EF-hand protein important for assembly of both the outer arm and the ODA-DC. Mol Biol Cell 14: 3650-3663, 2003.
    • (2003) Mol Biol Cell , vol.14 , pp. 3650-3663
    • Casey, D.M.1    Inaba, K.2    Pazour, G.J.3    Takada, S.4    Wakabayashi, K.5    Wilkerson, C.G.6    Kamiya, R.7    Witman, G.B.8
  • 5
    • 0142211197 scopus 로고    scopus 로고
    • DC3, the smallest subunit of the Chlamydomonas flagellar outer dynein arm-docking complex, is a redox-sensitive calcium-binding protein
    • Casey DM, Yagi T, Kamiya R, Witman GB. DC3, the smallest subunit of the Chlamydomonas flagellar outer dynein arm-docking complex, is a redox-sensitive calcium-binding protein. J Biol Chem 278: 42652-42659, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 42652-42659
    • Casey, D.M.1    Yagi, T.2    Kamiya, R.3    Witman, G.B.4
  • 7
    • 70449646115 scopus 로고    scopus 로고
    • The dynamic cilium in human diseases
    • D'Angelo A, Franco B. The dynamic cilium in human diseases. Pathogenetics 2: 3, 2009.
    • (2009) Pathogenetics , vol.2 , pp. 3
    • D'Angelo, A.1    Franco, B.2
  • 8
    • 77951114609 scopus 로고    scopus 로고
    • Calcium regulation of ciliary motility analysis of axonemal calcium-binding proteins
    • DiPetrillo C, Smith E. Calcium regulation of ciliary motility analysis of axonemal calcium-binding proteins. Methods Cell Biol 92: 163-180, 2009.
    • (2009) Methods Cell Biol , vol.92 , pp. 163-180
    • DiPetrillo, C.1    Smith, E.2
  • 9
    • 77951869322 scopus 로고    scopus 로고
    • Pcdp1 is a central apparatus protein that binds Ca(2+)-calmodulin and regulates ciliary motility
    • DiPetrillo CG, Smith EF. Pcdp1 is a central apparatus protein that binds Ca(2+)-calmodulin and regulates ciliary motility. J Cell Biol 189: 601- 612, 2010.
    • (2010) J Cell Biol , vol.189 , pp. 601-612
    • DiPetrillo, C.G.1    Smith, E.F.2
  • 10
    • 77956624120 scopus 로고    scopus 로고
    • The regulation of dynein-driven microtubule sliding in Chlamydomonas flagella by axonemal kinases and phosphatases
    • Elam CA, Sale WS, Wirschell M. The regulation of dynein-driven microtubule sliding in Chlamydomonas flagella by axonemal kinases and phosphatases. Methods Cell Biol 92: 133-151, 2009.
    • (2009) Methods Cell Biol , vol.92 , pp. 133-151
    • Elam, C.A.1    Sale, W.S.2    Wirschell, M.3
  • 13
    • 0035897417 scopus 로고    scopus 로고
    • Flagellar radial spoke protein 3 is an A-kinase anchoring protein (AKAP)
    • Gaillard AR, Diener DR, Rosenbaum JL, Sale WS. Flagellar radial spoke protein 3 is an A-kinase anchoring protein (AKAP). J Cell Biol 153: 443-448, 2001.
    • (2001) J Cell Biol , vol.153 , pp. 443-448
    • Gaillard, A.R.1    Diener, D.R.2    Rosenbaum, J.L.3    Sale, W.S.4
  • 14
    • 33744728042 scopus 로고    scopus 로고
    • Disruption of the A-kinase anchoring domain in flagellar radial spoke protein 3 results in unregulated axonemal cAMP-dependent protein kinase activity and abnormal flagellar motility
    • Gaillard AR, Fox LA, Rhea JM, Craige B, Sale WS. Disruption of the A-kinase anchoring domain in flagellar radial spoke protein 3 results in unregulated axonemal cAMP-dependent protein kinase activity and abnormal flagellar motility. Mol Biol Cell 17: 2626-2635, 2006.
    • (2006) Mol Biol Cell , vol.17 , pp. 2626-2635
    • Gaillard, A.R.1    Fox, L.A.2    Rhea, J.M.3    Craige, B.4    Sale, W.S.5
  • 15
    • 21244479076 scopus 로고    scopus 로고
    • The affinity of the dynein microtubule-binding domain is modulated by the conformation of its coiled-coil stalk
    • Gibbons IR, Garbarino JE, Tan CE, Reck-Peterson SL, Vale RD, Carter AP. The affinity of the dynein microtubule-binding domain is modulated by the conformation of its coiled-coil stalk. J Biol Chem 280: 23960-23965, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 23960-23965
    • Gibbons, I.R.1    Garbarino, J.E.2    Tan, C.E.3    Reck-Peterson, S.L.4    Vale, R.D.5    Carter, A.P.6
  • 16
    • 70349941538 scopus 로고    scopus 로고
    • Regulation of dynein-driven microtubule sliding by the axonemal protein kinase CK1 in Chlamydomonas flagella
    • Gokhale A, Wirschell M, Sale WS. Regulation of dynein-driven microtubule sliding by the axonemal protein kinase CK1 in Chlamydomonas flagella. J Cell Biol 186: 817-824, 2009.
    • (2009) J Cell Biol , vol.186 , pp. 817-824
    • Gokhale, A.1    Wirschell, M.2    Sale, W.S.3
  • 17
    • 0029890059 scopus 로고    scopus 로고
    • Regulation of flagellar dynein by an axonemal type-1 phosphatase in Chlamydomonas
    • Habermacher G, Sale WS. Regulation of flagellar dynein by an axonemal type-1 phosphatase in Chlamydomonas. J Cell Sci 109: 1899-1907, 1996.
    • (1996) J Cell Sci , vol.109 , pp. 1899-1907
    • Habermacher, G.1    Sale, W.S.2
  • 18
    • 84882905768 scopus 로고    scopus 로고
    • Chlamydomonas in the laboratory
    • edited by Harris E. Kidlington. Oxford, UK: Academic
    • Harris E. Chlamydomonas in the laboratory. In: The Chlamydomonas Sourcebook, edited by Harris E. Kidlington. Oxford, UK: Academic, 2009, p. 241-301.
    • (2009) The Chlamydomonas Sourcebook , pp. 241-301
    • Harris, E.1
  • 19
    • 84900422761 scopus 로고    scopus 로고
    • Picking up speed: Advances in the genetics of primary ciliary dyskinesia
    • Horani A, Brody SL, Ferkol TW. Picking up speed: advances in the genetics of primary ciliary dyskinesia. Pediatr Res 75: 158-164, 2014.
    • (2014) Pediatr Res , vol.75 , pp. 158-164
    • Horani, A.1    Brody, S.L.2    Ferkol, T.W.3
  • 20
    • 0020082250 scopus 로고
    • Suppressor mutations in Chlamydomonas reveal a regulatory mechanism for flagellar function
    • Huang B, Ramanis Z, Luck DJ. Suppressor mutations in Chlamydomonas reveal a regulatory mechanism for flagellar function. Cell 28: 115- 124, 1982.
    • (1982) Cell , vol.28 , pp. 115-124
    • Huang, B.1    Ramanis, Z.2    Luck, D.J.3
  • 21
    • 0020363859 scopus 로고
    • Survival after a serum ethanol concentration of 1 1/2%
    • Johnson RA, Noll EC, Rodney WM. Survival after a serum ethanol concentration of 1 1/2%. Lancet 2: 1394, 1982.
    • (1982) Lancet , vol.2 , pp. 1394
    • Johnson, R.A.1    Noll, E.C.2    Rodney, W.M.3
  • 22
    • 73349138284 scopus 로고    scopus 로고
    • Separation and detection of large phosphoproteins using Phos-tag SDS-PAGE
    • Kinoshita E, Kinoshita-Kikuta E, Koike T. Separation and detection of large phosphoproteins using Phos-tag SDS-PAGE. Nat Protoc 4: 1513- 1521, 2009.
    • (2009) Nat Protoc , vol.4 , pp. 1513-1521
    • Kinoshita, E.1    Kinoshita-Kikuta, E.2    Koike, T.3
  • 23
    • 69449098184 scopus 로고    scopus 로고
    • Mobility shift detection of phosphorylation on large proteins using a Phos-tag SDSPAGE gel strengthened with agarose
    • Kinoshita E, Kinoshita-Kikuta E, Ujihara H, Koike T. Mobility shift detection of phosphorylation on large proteins using a Phos-tag SDSPAGE gel strengthened with agarose. Proteomics 9: 4098-4101, 2009.
    • (2009) Proteomics , vol.9 , pp. 4098-4101
    • Kinoshita, E.1    Kinoshita-Kikuta, E.2    Ujihara, H.3    Koike, T.4
  • 25
    • 47049114331 scopus 로고    scopus 로고
    • Partially functional outer-arm dynein in a novel Chlamydomonas mutant expressing a truncated gamma heavy chain
    • Liu Z, Takazaki H, Nakazawa Y, Sakato M, Yagi T, Yasunaga T, King SM, Kamiya R. Partially functional outer-arm dynein in a novel Chlamydomonas mutant expressing a truncated gamma heavy chain. Eukaryot Cell 7: 1136-1145, 2008.
    • (2008) Eukaryot Cell , vol.7 , pp. 1136-1145
    • Liu, Z.1    Takazaki, H.2    Nakazawa, Y.3    Sakato, M.4    Yagi, T.5    Yasunaga, T.6    King, S.M.7    Kamiya, R.8
  • 26
    • 84865311801 scopus 로고    scopus 로고
    • Computerassisted image analysis of human cilia and Chlamydomonas flagella reveals both similarities and differences in axoneme structure
    • O'Toole ET, Giddings TH Jr, Porter ME, Ostrowski LE. Computerassisted image analysis of human cilia and Chlamydomonas flagella reveals both similarities and differences in axoneme structure. Cytoskeleton (Hoboken) 69: 577-590, 2012.
    • (2012) Cytoskeleton (Hoboken) , vol.69 , pp. 577-590
    • O'Toole, E.T.1    Giddings, T.H.2    Porter, M.E.3    Ostrowski, L.E.4
  • 28
    • 44049107514 scopus 로고    scopus 로고
    • Cilia and ciliopathies: From Chlamydomonas and beyond
    • Pan J. Cilia and ciliopathies: from Chlamydomonas and beyond. Sci China C Life Sci 51: 479-486, 2008.
    • (2008) Sci China C Life Sci , vol.51 , pp. 479-486
    • Pan, J.1
  • 30
    • 0028040415 scopus 로고
    • Mutations in the SUP-PF-1 locus of Chlamydomonas reinhardtii identify a regulatory domain in the beta-dynein heavy chain
    • Porter ME, Knott JA, Gardner LC, Mitchell DR, Dutcher SK. Mutations in the SUP-PF-1 locus of Chlamydomonas reinhardtii identify a regulatory domain in the beta-dynein heavy chain. J Cell Biol 126: 1495-1507, 1994.
    • (1994) J Cell Biol , vol.126 , pp. 1495-1507
    • Porter, M.E.1    Knott, J.A.2    Gardner, L.C.3    Mitchell, D.R.4    Dutcher, S.K.5
  • 31
    • 0034722338 scopus 로고    scopus 로고
    • The 9 + 2 axoneme anchors multiple inner arm dyneins and a network of kinases and phosphatases that control motility
    • Porter ME, Sale WS. The 9 + 2 axoneme anchors multiple inner arm dyneins and a network of kinases and phosphatases that control motility. J Cell Biol 151: F37-F42, 2000.
    • (2000) J Cell Biol , vol.151 , pp. F37-F42
    • Porter, M.E.1    Sale, W.S.2
  • 33
    • 0030463112 scopus 로고    scopus 로고
    • The sup-pf-2 mutations of Chlamydomonas alter the activity of the outer dynein arms by modification of the gamma-dynein heavy chain
    • Rupp G, O'Toole E, Gardner LC, Mitchell BF, Porter ME. The sup-pf-2 mutations of Chlamydomonas alter the activity of the outer dynein arms by modification of the gamma-dynein heavy chain. J Cell Biol 135: 1853-1865, 1996.
    • (1996) J Cell Biol , vol.135 , pp. 1853-1865
    • Rupp, G.1    O'Toole, E.2    Gardner, L.C.3    Mitchell, B.F.4    Porter, M.E.5
  • 34
    • 0025894163 scopus 로고
    • A Chlamydomonas outer arm dynein mutant missing the alpha heavy chain
    • Sakakibara H, Mitchell DR, Kamiya R. A Chlamydomonas outer arm dynein mutant missing the alpha heavy chain. J Cell Biol 113: 615-622, 1991.
    • (1991) J Cell Biol , vol.113 , pp. 615-622
    • Sakakibara, H.1    Mitchell, D.R.2    Kamiya, R.3
  • 35
    • 0027183187 scopus 로고
    • A Chlamydomonas outer arm dynein mutant with a truncated beta heavy chain
    • Sakakibara H, Takada S, King SM, Witman GB, Kamiya R. A Chlamydomonas outer arm dynein mutant with a truncated beta heavy chain. J Cell Biol 122: 653-661, 1993.
    • (1993) J Cell Biol , vol.122 , pp. 653-661
    • Sakakibara, H.1    Takada, S.2    King, S.M.3    Witman, G.B.4    Kamiya, R.5
  • 36
    • 58149326842 scopus 로고    scopus 로고
    • Ciliary dysfunction in developmental abnormalities and diseases
    • Sharma N, Berbari NF, Yoder BK. Ciliary dysfunction in developmental abnormalities and diseases. Curr Top Dev Biol 85: 371-427, 2008.
    • (2008) Curr Top Dev Biol , vol.85 , pp. 371-427
    • Sharma, N.1    Berbari, N.F.2    Yoder, B.K.3
  • 38
    • 0028911219 scopus 로고
    • Ethanol stimulates apparent nitric oxide-dependent ciliary beat frequency in bovine airway epithelial cells
    • Sisson JH. Ethanol stimulates apparent nitric oxide-dependent ciliary beat frequency in bovine airway epithelial cells. Am J Physiol Lung Cell Mol Physiol 268: L596-L600, 1995.
    • (1995) Am J Physiol Lung Cell Mol Physiol , vol.268 , pp. L596-L600
    • Sisson, J.H.1
  • 39
    • 0032880645 scopus 로고    scopus 로고
    • Nitric oxide-dependent ethanol stimulation of ciliary motility is linked to cAMP-dependent protein kinase (PKA) activation in bovine bronchial epithelium
    • Sisson JH, May K, Wyatt TA. Nitric oxide-dependent ethanol stimulation of ciliary motility is linked to cAMP-dependent protein kinase (PKA) activation in bovine bronchial epithelium. Alcohol Clin Exp Res 23: 1528-1533, 1999.
    • (1999) Alcohol Clin Exp Res , vol.23 , pp. 1528-1533
    • Sisson, J.H.1    May, K.2    Wyatt, T.A.3
  • 40
    • 63149128130 scopus 로고    scopus 로고
    • Alcohol stimulates ciliary motility of isolated airway axonemes through a nitric oxide, cyclase, and cyclic nucleotide-dependent kinase mechanism
    • Sisson JH, Pavlik JA, Wyatt TA. Alcohol stimulates ciliary motility of isolated airway axonemes through a nitric oxide, cyclase, and cyclic nucleotide-dependent kinase mechanism. Alcohol Clin Exp Res 33: 610- 616, 2009.
    • (2009) Alcohol Clin Exp Res , vol.33 , pp. 610-616
    • Sisson, J.H.1    Pavlik, J.A.2    Wyatt, T.A.3
  • 41
    • 0041657684 scopus 로고    scopus 로고
    • All-digital image capture and whole-field analysis of ciliary beat frequency
    • Sisson JH, Stoner JA, Ammons BA, Wyatt TA. All-digital image capture and whole-field analysis of ciliary beat frequency. J Microsc 211: 103-111, 2003.
    • (2003) J Microsc , vol.211 , pp. 103-111
    • Sisson, J.H.1    Stoner, J.A.2    Ammons, B.A.3    Wyatt, T.A.4
  • 43
    • 0036732941 scopus 로고    scopus 로고
    • Regulation of flagellar dynein by calcium and a role for an axonemal calmodulin and calmodulin-dependent kinase
    • Smith EF. Regulation of flagellar dynein by calcium and a role for an axonemal calmodulin and calmodulin-dependent kinase. Mol Biol Cell 13: 3303-3313, 2002.
    • (2002) Mol Biol Cell , vol.13 , pp. 3303-3313
    • Smith, E.F.1
  • 44
    • 0027953834 scopus 로고
    • Functional reconstitution of Chlamydomonas outer dynein arms from alpha-beta and gamma subunits: Requirement of a third factor
    • Takada S, Kamiya R. Functional reconstitution of Chlamydomonas outer dynein arms from alpha-beta and gamma subunits: requirement of a third factor. J Cell Biol 126: 737-745, 1994.
    • (1994) J Cell Biol , vol.126 , pp. 737-745
    • Takada, S.1    Kamiya, R.2
  • 45
    • 0036199035 scopus 로고    scopus 로고
    • The outer dynein arm-docking complex: Composition and characterization of a subunit (oda1) necessary for outer arm assembly
    • Takada S, Wilkerson CG, Wakabayashi K, Kamiya R, Witman GB. The outer dynein arm-docking complex: composition and characterization of a subunit (oda1) necessary for outer arm assembly. Mol Biol Cell 13: 1015-1029, 2002.
    • (2002) Mol Biol Cell , vol.13 , pp. 1015-1029
    • Takada, S.1    Wilkerson, C.G.2    Wakabayashi, K.3    Kamiya, R.4    Witman, G.B.5
  • 46
    • 0024452140 scopus 로고
    • Blood alcohol level among emergency room patients: A multivariate analysis
    • Teplin LA, Abram KM, Michaels SK. Blood alcohol level among emergency room patients: a multivariate analysis. J Stud Alcohol 50: 441-447, 1989.
    • (1989) J Stud Alcohol , vol.50 , pp. 441-447
    • Teplin, L.A.1    Abram, K.M.2    Michaels, S.K.3
  • 47
    • 27844496997 scopus 로고    scopus 로고
    • Calmodulin and PF6 are components of a complex that localizes to the C1 microtubule of the flagellar central apparatus
    • Wargo MJ, Dymek EE, Smith EF. Calmodulin and PF6 are components of a complex that localizes to the C1 microtubule of the flagellar central apparatus. J Cell Sci 118: 4655-4665, 2005.
    • (2005) J Cell Sci , vol.118 , pp. 4655-4665
    • Wargo, M.J.1    Dymek, E.E.2    Smith, E.F.3
  • 48
    • 80052446941 scopus 로고    scopus 로고
    • Ciliopathies: An expanding disease spectrum
    • Waters AM, Beales PL. Ciliopathies: an expanding disease spectrum. Pediatr Nephrol 26: 1039-1056, 2011.
    • (2011) Pediatr Nephrol , vol.26 , pp. 1039-1056
    • Waters, A.M.1    Beales, P.L.2
  • 49
    • 34547104215 scopus 로고    scopus 로고
    • Keeping an eye on I1: I1 dynein as a model for flagellar dynein assembly and regulation
    • Wirschell M, Hendrickson T, Sale WS. Keeping an eye on I1: I1 dynein as a model for flagellar dynein assembly and regulation. Cell Motil Cytoskeleton 64: 569-579, 2007.
    • (2007) Cell Motil Cytoskeleton , vol.64 , pp. 569-579
    • Wirschell, M.1    Hendrickson, T.2    Sale, W.S.3
  • 51
    • 79958717871 scopus 로고    scopus 로고
    • Regulation of ciliary motility: Conserved protein kinases and phosphatases are targeted and anchored in the ciliary axoneme
    • Wirschell M, Yamamoto R, Alford L, Gokhale A, Gaillard A, Sale WS. Regulation of ciliary motility: Conserved protein kinases and phosphatases are targeted and anchored in the ciliary axoneme. Arch Biochem Biophys 510: 93-100, 2011.
    • (2011) Arch Biochem Biophys , vol.510 , pp. 93-100
    • Wirschell, M.1    Yamamoto, R.2    Alford, L.3    Gokhale, A.4    Gaillard, A.5    Sale, W.S.6
  • 52
    • 0022962478 scopus 로고
    • Isolation of Chlamydomonas flagella and flagellar axonemes
    • Witman GB. Isolation of Chlamydomonas flagella and flagellar axonemes. Methods Enzymol 134: 280-290, 1986.
    • (1986) Methods Enzymol , vol.134 , pp. 280-290
    • Witman, G.B.1
  • 53
    • 0034822763 scopus 로고    scopus 로고
    • Chronic ethanol downregulates PKA activation and ciliary beating in bovine bronchial epithelial cells
    • Wyatt TA, Sisson JH. Chronic ethanol downregulates PKA activation and ciliary beating in bovine bronchial epithelial cells. Am J Physiol Lung Cell Mol Physiol 281: L575-L581, 2001.
    • (2001) Am J Physiol Lung Cell Mol Physiol , vol.281 , pp. L575-L581
    • Wyatt, T.A.1    Sisson, J.H.2
  • 54
    • 0033967129 scopus 로고    scopus 로고
    • Protein phosphatases PP1 and PP2A are located in distinct positions in the Chlamydomonas flagellar axoneme
    • Yang P, Fox L, Colbran RJ, Sale WS. Protein phosphatases PP1 and PP2A are located in distinct positions in the Chlamydomonas flagellar axoneme. J Cell Sci 113: 91-102, 2000.
    • (2000) J Cell Sci , vol.113 , pp. 91-102
    • Yang, P.1    Fox, L.2    Colbran, R.J.3    Sale, W.S.4


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