메뉴 건너뛰기




Volumn 11, Issue , 2005, Pages 1061-1070

The regulatory subunit of PDE6 interacts with PACSIN in photoreceptors

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CELL PROTEIN; FORMIN BINDING PROTEIN 17; GLUTATHIONE TRANSFERASE; PACSIN; PHOSPHODIESTERASE; PHOSPHODIESTERASE VI; POLYAMINOACID; PROLINE; PROTEIN SH2; PROTEIN SH3; PROTEIN SUBUNIT; TRANSDUCIN; UNCLASSIFIED DRUG;

EID: 29244446227     PISSN: 10900535     EISSN: 10900535     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (19)

References (49)
  • 1
    • 0028332848 scopus 로고
    • Transduction mechanisms of vertebrate and invertebrate photoreceptors
    • Yarfitz S, Hurley JB. Transduction mechanisms of vertebrate and invertebrate photoreceptors. J Biol Chem 1994; 269:14329-32.
    • (1994) J Biol Chem , vol.269 , pp. 14329-14332
    • Yarfitz, S.1    Hurley, J.B.2
  • 2
    • 84943251864 scopus 로고    scopus 로고
    • Structure, function, and regulation of photoreceptor phosphodiesterase (PDE6)
    • Bradshaw RA, Dennis EA, editors. San Diego: Academic Press
    • Cote RH. Structure, function, and regulation of photoreceptor phosphodiesterase (PDE6). In: Bradshaw RA, Dennis EA, editors. Handbook of cell signaling. San Diego: Academic Press; 2004. p. 453-7.
    • (2004) Handbook of Cell Signaling , pp. 453-457
    • Cote, R.H.1
  • 4
    • 0028979355 scopus 로고
    • The carboxyl terminus of the gamma-subunit of rod cGMP phosphodiesterase contains distinct sites of interaction with the enzyme catalytic subunits and the alpha-subunit of transducin
    • Skiba NP, Artemyev NO, Hamm HE. The carboxyl terminus of the gamma-subunit of rod cGMP phosphodiesterase contains distinct sites of interaction with the enzyme catalytic subunits and the alpha-subunit of transducin. J Biol Chem 1995; 270:13210-5.
    • (1995) J Biol Chem , vol.270 , pp. 13210-13215
    • Skiba, N.P.1    Artemyev, N.O.2    Hamm, H.E.3
  • 5
    • 0023713635 scopus 로고
    • Active sites of the cyclic GMP phosphodiesterase gamma-subunit of retinal rod outer segments
    • Lipkin VM, Dumler IL, Muradov KG, Artemyev NO, Etingof RN. Active sites of the cyclic GMP phosphodiesterase gamma-subunit of retinal rod outer segments. FEBS Lett 1988; 234:287-90.
    • (1988) FEBS Lett , vol.234 , pp. 287-290
    • Lipkin, V.M.1    Dumler, I.L.2    Muradov, K.G.3    Artemyev, N.O.4    Etingof, R.N.5
  • 6
    • 0026780630 scopus 로고
    • Functional regions of the inhibitory subunit of retinal rod cGMP phosphodiesterase identified by site-specific mutagenesis and fluorescence spectroscopy
    • Brown RL. Functional regions of the inhibitory subunit of retinal rod cGMP phosphodiesterase identified by site-specific mutagenesis and fluorescence spectroscopy. Biochemistry 1992; 31:5918-25.
    • (1992) Biochemistry , vol.31 , pp. 5918-5925
    • Brown, R.L.1
  • 7
    • 0030972213 scopus 로고    scopus 로고
    • The gamma subunit of rod cGMP-phosphodiesterase blocks the enzyme catalytic site
    • Granovsky AE, Natochin M, Artemyev NO. The gamma subunit of rod cGMP-phosphodiesterase blocks the enzyme catalytic site. J Biol Chem 1997; 272:11686-9.
    • (1997) J Biol Chem , vol.272 , pp. 11686-11689
    • Granovsky, A.E.1    Natochin, M.2    Artemyev, N.O.3
  • 8
    • 0024514907 scopus 로고
    • G protein-effector coupling: Binding of rod phosphodiesterase inhibitory subunit to transducin
    • Fung BK, Griswold-Prenner I. G protein-effector coupling: binding of rod phosphodiesterase inhibitory subunit to transducin. Biochemistry 1989; 28:3133-7.
    • (1989) Biochemistry , vol.28 , pp. 3133-3137
    • Fung, B.K.1    Griswold-Prenner, I.2
  • 9
    • 0024389435 scopus 로고
    • Interaction of the gamma-subunit of retinal rod outer segment phosphodiesterase with transducin. Use of synthetic peptides as functional probes
    • Morrison DF, Cunnick JM, Oppert B, Takemoto DJ. Interaction of the gamma-subunit of retinal rod outer segment phosphodiesterase with transducin. Use of synthetic peptides as functional probes. J Biol Chem 1989; 264:11671-81.
    • (1989) J Biol Chem , vol.264 , pp. 11671-11681
    • Morrison, D.F.1    Cunnick, J.M.2    Oppert, B.3    Takemoto, D.J.4
  • 10
    • 0347093423 scopus 로고    scopus 로고
    • A proline-rich domain in the gamma subunit of phosphodiesterase 6 mediates interaction with SH3-containing proteins
    • Erratum in: Mol Vis 2003; 9:449
    • Morin F, Vannier B, Houdart F, Regnacq M, Berges T, Voisin P. A proline-rich domain in the gamma subunit of phosphodiesterase 6 mediates interaction with SH3-containing proteins. Mol Vis 2003; 9:449-59. Erratum in: Mol Vis 2003; 9:449.
    • (2003) Mol Vis , vol.9 , pp. 449-459
    • Morin, F.1    Vannier, B.2    Houdart, F.3    Regnacq, M.4    Berges, T.5    Voisin, P.6
  • 11
    • 0037342368 scopus 로고    scopus 로고
    • Receptor tyrosine kinase and G-protein coupled receptor signaling and sorting within endosomes
    • Grimes ML, Miettinen HM. Receptor tyrosine kinase and G-protein coupled receptor signaling and sorting within endosomes. J Neurochem 2003; 84:905-18.
    • (2003) J Neurochem , vol.84 , pp. 905-918
    • Grimes, M.L.1    Miettinen, H.M.2
  • 13
    • 4544251239 scopus 로고    scopus 로고
    • A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis
    • Kamioka Y, Fukuhara S, Sawa H, Nagashima K, Masuda M, Matsuda M, Mochizuki N. A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis. J Biol Chem 2004; 279:40091-9.
    • (2004) J Biol Chem , vol.279 , pp. 40091-40099
    • Kamioka, Y.1    Fukuhara, S.2    Sawa, H.3    Nagashima, K.4    Masuda, M.5    Matsuda, M.6    Mochizuki, N.7
  • 14
    • 0035851113 scopus 로고    scopus 로고
    • The inhibitory gamma subunit of the type 6 retinal cyclic guanosine monophosphate phosphodiesterase is a novel intermediate regulating p42/p44 mitogen-activated protein kinase signaling in human embryonic kidney 293 cells
    • Wan KF, Sambi BS, Frame M, Tate R, Pyne NJ. The inhibitory gamma subunit of the type 6 retinal cyclic guanosine monophosphate phosphodiesterase is a novel intermediate regulating p42/p44 mitogen-activated protein kinase signaling in human embryonic kidney 293 cells. J Biol Chem 2001; 276:37802-8.
    • (2001) J Biol Chem , vol.276 , pp. 37802-37808
    • Wan, K.F.1    Sambi, B.S.2    Frame, M.3    Tate, R.4    Pyne, N.J.5
  • 15
    • 0004086785 scopus 로고
    • Methods for cloning and analysis of eukaryotic genes
    • Boston: Jones and Bartlett
    • Bothwell A, Yancopoulos GD, Alt FW. Methods for cloning and analysis of eukaryotic genes. Boston: Jones and Bartlett; 1990.
    • (1990)
    • Bothwell, A.1    Yancopoulos, G.D.2    Alt, F.W.3
  • 17
    • 0016370981 scopus 로고
    • Visual pathways and the central neural control of a circadian rhythm in pineal serotonin N-acetyltransferase activity
    • Moore RY, Klein DC. Visual pathways and the central neural control of a circadian rhythm in pineal serotonin N-acetyltransferase activity. Brain Res 1974; 71:17-33.
    • (1974) Brain Res , vol.71 , pp. 17-33
    • Moore, R.Y.1    Klein, D.C.2
  • 20
    • 0034503124 scopus 로고    scopus 로고
    • All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis
    • Modregger J, Ritter B, Witter B, Paulsson M, Plomann M. All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis. J Cell Sci 2000; 113 Pt 24:4511-21.
    • (2000) J Cell Sci , vol.113 , Issue.PART 24 , pp. 4511-4521
    • Modregger, J.1    Ritter, B.2    Witter, B.3    Paulsson, M.4    Plomann, M.5
  • 21
    • 0034636685 scopus 로고    scopus 로고
    • Regulation of mitogen-activated protein kinase signaling networks by G protein-coupled receptors
    • Gutkind JS. Regulation of mitogen-activated protein kinase signaling networks by G protein-coupled receptors. Sci STKE 2000; 2000:RE1.
    • (2000) Sci STKE , vol.2000
    • Gutkind, J.S.1
  • 23
    • 0023114097 scopus 로고
    • Diurnal expression of transducin mRNA and translocation of transducin in rods of rat retina
    • Brann MR, Cohen LV. Diurnal expression of transducin mRNA and translocation of transducin in rods of rat retina. Science 1987; 235:585-7.
    • (1987) Science , vol.235 , pp. 585-587
    • Brann, M.R.1    Cohen, L.V.2
  • 24
    • 0037187644 scopus 로고    scopus 로고
    • Massive light-driven translocation of transducin between the two major compartments of rod cells: A novel mechanism of light adaptation
    • Sokolov M, Lyubarsky AL, Strissel KJ, Savchenko AB, Govardovskii VI, Pugh EN Jr, Arshavsky VY. Massive light-driven translocation of transducin between the two major compartments of rod cells: a novel mechanism of light adaptation. Neuron 2002; 34:95-106.
    • (2002) Neuron , vol.34 , pp. 95-106
    • Sokolov, M.1    Lyubarsky, A.L.2    Strissel, K.J.3    Savchenko, A.B.4    Govardovskii, V.I.5    Pugh Jr., E.N.6    Arshavsky, V.Y.7
  • 25
    • 0037847499 scopus 로고    scopus 로고
    • Light-dependent translocation of arrestin in the absence of rhodopsin phosphorylation and transducin signaling
    • Mendez A, Lem J, Simon M, Chen J. Light-dependent translocation of arrestin in the absence of rhodopsin phosphorylation and transducin signaling. J Neurosci 2003; 23:3124-9.
    • (2003) J Neurosci , vol.23 , pp. 3124-3129
    • Mendez, A.1    Lem, J.2    Simon, M.3    Chen, J.4
  • 26
    • 0038071520 scopus 로고    scopus 로고
    • Light-dependent redistribution of visual arrestins and transducin subunits in mice with defective phototransduction
    • Zhang H, Huang W, Zhang H, Zhu X, Craft CM, Baehr W, Chen CK. Light-dependent redistribution of visual arrestins and transducin subunits in mice with defective phototransduction. Mol Vis 2003; 9:231-7.
    • (2003) Mol Vis , vol.9 , pp. 231-237
    • Zhang, H.1    Huang, W.2    Zhang, H.3    Zhu, X.4    Craft, C.M.5    Baehr, W.6    Chen, C.K.7
  • 27
    • 14844328342 scopus 로고    scopus 로고
    • Temporal kinetics of the light/dark translocation and compartmentation of arrestin and alpha-transducin in mouse photoreceptor cells
    • Elias RV, Sezate SS, Cao W, McGinnis JF. Temporal kinetics of the light/dark translocation and compartmentation of arrestin and alpha-transducin in mouse photoreceptor cells. Mol Vis 2004; 10:672-81.
    • (2004) Mol Vis , vol.10 , pp. 672-681
    • Elias, R.V.1    Sezate, S.S.2    Cao, W.3    McGinnis, J.F.4
  • 28
    • 0034605038 scopus 로고    scopus 로고
    • Molecular links between endocytosis and the actin cytoskeleton
    • Qualmann B, Kessels MM, Kelly RB. Molecular links between endocytosis and the actin cytoskeleton. J Cell Biol 2000; 150:F111-6.
    • (2000) J Cell Biol , vol.150
    • Qualmann, B.1    Kessels, M.M.2    Kelly, R.B.3
  • 29
    • 0018595710 scopus 로고
    • Isolation and characterization of cGMP phosphodiesterase from bovine rod outer segments
    • Baehr W, Devlin MJ, Applebury ML. Isolation and characterization of cGMP phosphodiesterase from bovine rod outer segments. J Biol Chem 1979; 254:11669-77.
    • (1979) J Biol Chem , vol.254 , pp. 11669-11677
    • Baehr, W.1    Devlin, M.J.2    Applebury, M.L.3
  • 30
    • 0020356005 scopus 로고
    • Purification and characterization of the gamma regulatory subunit of the cyclic GMP phosphodiesterase from retinal rod outer segments
    • Hurley JB, Stryer L. Purification and characterization of the gamma regulatory subunit of the cyclic GMP phosphodiesterase from retinal rod outer segments. J Biol Chem 1982; 257:11094-9.
    • (1982) J Biol Chem , vol.257 , pp. 11094-11099
    • Hurley, J.B.1    Stryer, L.2
  • 31
  • 32
    • 0030741537 scopus 로고    scopus 로고
    • The regulation of the cGMP-binding cGMP phosphodiesterase by proteins that are immunologically related to gamma subunit of the photoreceptor cGMP phosphodiesterase
    • Lochhead A, Nekrasova E, Arshavsky VY, Pyne NJ. The regulation of the cGMP-binding cGMP phosphodiesterase by proteins that are immunologically related to gamma subunit of the photoreceptor cGMP phosphodiesterase. J Biol Chem 1997; 272:18397-403.
    • (1997) J Biol Chem , vol.272 , pp. 18397-18403
    • Lochhead, A.1    Nekrasova, E.2    Arshavsky, V.Y.3    Pyne, N.J.4
  • 33
    • 0036203862 scopus 로고    scopus 로고
    • The identification of the inhibitory gamma-subunits of the type 6 retinal cyclic guanosine monophosphate phosphodiesterase in non-retinal tissues: Differential processing of mRNA transcripts
    • Erratum in: Genomics 2004; 83:346
    • Tate RJ, Arshavsky VY, Pyne NJ. The identification of the inhibitory gamma-subunits of the type 6 retinal cyclic guanosine monophosphate phosphodiesterase in non-retinal tissues: differential processing of mRNA transcripts. Genomics 2002; 79:582-6. Erratum in: Genomics 2004; 83:346.
    • (2002) Genomics , vol.79 , pp. 582-586
    • Tate, R.J.1    Arshavsky, V.Y.2    Pyne, N.J.3
  • 34
    • 0037059804 scopus 로고    scopus 로고
    • Light-dependent association of Src with photoreceptor rod outer segment membrane proteins in vivo
    • Ghalayini AJ, Desai N, Smith KR, Holbrook RM, Elliott MH, Kawakatsu H. Light-dependent association of Src with photoreceptor rod outer segment membrane proteins in vivo. J Biol Chem 2002; 277:1469-76.
    • (2002) J Biol Chem , vol.277 , pp. 1469-1476
    • Ghalayini, A.J.1    Desai, N.2    Smith, K.R.3    Holbrook, R.M.4    Elliott, M.H.5    Kawakatsu, H.6
  • 35
    • 24044447239 scopus 로고    scopus 로고
    • Evidence that dystroglycan is associated with dynamin and regulates endocytosis
    • Zhan Y, Tremblay MR, Melian N, Carbonetto S. Evidence that dystroglycan is associated with dynamin and regulates endocytosis. J Biol Chem 2005; 280:18015-24.
    • (2005) J Biol Chem , vol.280 , pp. 18015-18024
    • Zhan, Y.1    Tremblay, M.R.2    Melian, N.3    Carbonetto, S.4
  • 36
    • 0025778534 scopus 로고
    • Phosphatidylinositol-stimulated phosphorylation of an inhibitory subunit of cGMP phosphodiesterase in vertebrate rod photoreceptors
    • Hayashi F, Lin GY, Matsumoto H, Yamazaki A. Phosphatidylinositol-stimulated phosphorylation of an inhibitory subunit of cGMP phosphodiesterase in vertebrate rod photoreceptors. Proc Natl Acad Sci U S A 1991; 88:4333-7.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 4333-4337
    • Hayashi, F.1    Lin, G.Y.2    Matsumoto, H.3    Yamazaki, A.4
  • 37
    • 0027433147 scopus 로고
    • Phosphorylation of bovine rod photoreceptor cyclic GMP phosphodiesterase
    • Udovichenko IP, Cunnick J, Gonzales K, Takemoto DJ. Phosphorylation of bovine rod photoreceptor cyclic GMP phosphodiesterase. Biochem J 1993; 295:49-55.
    • (1993) Biochem J , vol.295 , pp. 49-55
    • Udovichenko, I.P.1    Cunnick, J.2    Gonzales, K.3    Takemoto, D.J.4
  • 39
    • 0037085477 scopus 로고    scopus 로고
    • Regulation of photoreceptor phosphodiesterase (PDE6) by phosphorylation of its inhibitory gamma subunit re-evaluated
    • Paglia MJ, Mou H, Cote RH. Regulation of photoreceptor phosphodiesterase (PDE6) by phosphorylation of its inhibitory gamma subunit re-evaluated. J Biol Chem 2002; 277:5017-23.
    • (2002) J Biol Chem , vol.277 , pp. 5017-5023
    • Paglia, M.J.1    Mou, H.2    Cote, R.H.3
  • 41
    • 12544255192 scopus 로고    scopus 로고
    • Evaluation of the 17-kDa prenyl-binding protein as a regulatory protein for phototransduction in retinal photoreceptors
    • Norton AW, Hosier S, Terew JM, Li N, Dhingra A, Vardi N, Baehr W, Cote RH. Evaluation of the 17-kDa prenyl-binding protein as a regulatory protein for phototransduction in retinal photoreceptors. J Biol Chem 2005; 280:1248-56.
    • (2005) J Biol Chem , vol.280 , pp. 1248-1256
    • Norton, A.W.1    Hosier, S.2    Terew, J.M.3    Li, N.4    Dhingra, A.5    Vardi, N.6    Baehr, W.7    Cote, R.H.8
  • 43
    • 0035834983 scopus 로고    scopus 로고
    • PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the pacsin-syndapin-FAP52 gene family
    • Sumoy L, Pluvinet R, Andreu N, Estivill X, Escarceller M. PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the pacsin-syndapin-FAP52 gene family. Gene 2001; 262:199-205.
    • (2001) Gene , vol.262 , pp. 199-205
    • Sumoy, L.1    Pluvinet, R.2    Andreu, N.3    Estivill, X.4    Escarceller, M.5
  • 44
    • 2342501822 scopus 로고    scopus 로고
    • Localized expression of amphiphysin Ir, a retina-specific variant of amphiphysin I, in the ribbon synapse and its functional implication
    • Hosoya O, Tsutsui K, Tsutsui K. Localized expression of amphiphysin Ir, a retina-specific variant of amphiphysin I, in the ribbon synapse and its functional implication. Eur J Neurosci 2004; 19:2179-87.
    • (2004) Eur J Neurosci , vol.19 , pp. 2179-2187
    • Hosoya, O.1    Tsutsui, K.2    Tsutsui, K.3
  • 45
    • 0027460742 scopus 로고
    • Expression of mouse rod photoreceptor cGMP phosphodiesterase gamma subunit in bacteria
    • Qin N, Baehr W. Expression of mouse rod photoreceptor cGMP phosphodiesterase gamma subunit in bacteria. FEBS Lett 1993; 321:6-10.
    • (1993) FEBS Lett , vol.321 , pp. 6-10
    • Qin, N.1    Baehr, W.2
  • 46
    • 11144256172 scopus 로고    scopus 로고
    • Structure and function of ribbon synapses
    • Sterling P, Matthews G. Structure and function of ribbon synapses. Trends Neurosci 2005; 28:20-9.
    • (2005) Trends Neurosci , vol.28 , pp. 20-29
    • Sterling, P.1    Matthews, G.2
  • 47
    • 0023628488 scopus 로고
    • Endocytosis in the inner segment of rod photoreceptors: Analysis of Xenopus laevis retinas using horseradish peroxidase
    • Hollyfield JG, Rayborn ME. Endocytosis in the inner segment of rod photoreceptors: analysis of Xenopus laevis retinas using horseradish peroxidase. Exp Eye Res 1987; 45:703-19.
    • (1987) Exp Eye Res , vol.45 , pp. 703-719
    • Hollyfield, J.G.1    Rayborn, M.E.2
  • 48
    • 5444268144 scopus 로고    scopus 로고
    • The zebrafish nrc mutant reveals a role for the polyphosphoinositide phosphatase synaptojanin 1 in cone photoreceptor ribbon anchoring
    • Van Epps HA, Hayashi M, Lucast L, Stearns GW, Hurley JB, De Camilli P, Brockerhoff SE. The zebrafish nrc mutant reveals a role for the polyphosphoinositide phosphatase synaptojanin 1 in cone photoreceptor ribbon anchoring. J Neurosci 2004; 24:8641-50.
    • (2004) J Neurosci , vol.24 , pp. 8641-8650
    • Van Epps, H.A.1    Hayashi, M.2    Lucast, L.3    Stearns, G.W.4    Hurley, J.B.5    De Camilli, P.6    Brockerhoff, S.E.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.