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Volumn 303, Issue 1, 2003, Pages 19-23

Active transducin α subunit carries PDE6 to detergent-resistant membranes in rod photoreceptor outer segments

Author keywords

DRM; Lipid raft; PDE6; Phosphodiesterase; Photoreceptor; Phototransduction; Rod outer segment; Transducin

Indexed keywords

ALUMINUM FLUORIDE; CYCLIC GMP PHOSPHODIESTERASE; PERTUSSIS TOXIN; REACTIVE OXYGEN METABOLITE; TRANSDUCIN; DETERGENT; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); PHOSPHATE; PHOSPHODIESTERASE; PHOSPHODIESTERASE 6;

EID: 0037470775     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00284-5     Document Type: Article
Times cited : (17)

References (19)
  • 1
    • 0027430227 scopus 로고
    • A GTPase-accelerating factor for transducin, distinct from its effector cGMP phosphodiesterase, in rod outer segment membranes
    • Angleson J.K., Wensel T.G. A GTPase-accelerating factor for transducin, distinct from its effector cGMP phosphodiesterase, in rod outer segment membranes. Neuron. 11:1993;939-949.
    • (1993) Neuron , vol.11 , pp. 939-949
    • Angleson, J.K.1    Wensel, T.G.2
  • 2
    • 0028340572 scopus 로고
    • Enhancement of rod outer segment GTPase accelerating protein activity by the inhibitory subunit of cGMP phosphodiesterase
    • Angleson J.K., Wensel T.G. Enhancement of rod outer segment GTPase accelerating protein activity by the inhibitory subunit of cGMP phosphodiesterase. J. Biol. Chem. 269:1994;16290-16296.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16290-16296
    • Angleson, J.K.1    Wensel, T.G.2
  • 4
    • 0031936503 scopus 로고    scopus 로고
    • RGS9, a GTPase accelerator for phototransduction
    • He W., Cowan C.W., Wensel T.G. RGS9, a GTPase accelerator for phototransduction. Neuron. 20:1998;95-102.
    • (1998) Neuron , vol.20 , pp. 95-102
    • He, W.1    Cowan, C.W.2    Wensel, T.G.3
  • 5
    • 0035877768 scopus 로고    scopus 로고
    • ′ -3-O-(thio)triphosphate-sensitive localization of a G protein and its effector on detergent-resistant membrane rafts in rod photoreceptor outer segments
    • ′ -3-O-(thio)triphosphate-sensitive localization of a G protein and its effector on detergent-resistant membrane rafts in rod photoreceptor outer segments J. Biol. Chem. 276:2001;20813-20816.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20813-20816
    • Seno, K.1    Kishimoto, M.2    Abe, M.3    Higuchi, Y.4    Mieda, M.5    Owada, Y.6    Yoshiyama, W.7    Liu, H.8    Hayashi, F.9
  • 7
  • 8
    • 0026495323 scopus 로고
    • Functional modifications of transducin induced by cholera or pertussis-toxin-catalyzed ADP-ribosylation
    • Bornancin F., Franco M., Bigay J., Chabre M. Functional modifications of transducin induced by cholera or pertussis-toxin-catalyzed ADP-ribosylation. Eur. J. Biochem. 210:1992;33-44.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 33-44
    • Bornancin, F.1    Franco, M.2    Bigay, J.3    Chabre, M.4
  • 9
    • 16944363275 scopus 로고    scopus 로고
    • Possible stimulation of retinal rod recovery to dark state by cGMP release from a cGMP phosphodiesterase noncatalytic site
    • Yamazaki A., Bondarenko V.A., Dua S., Yamazaki M., Usukura J., Hayashi F. Possible stimulation of retinal rod recovery to dark state by cGMP release from a cGMP phosphodiesterase noncatalytic site. J. Biol. Chem. 271:1996;32495-32498.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32495-32498
    • Yamazaki, A.1    Bondarenko, V.A.2    Dua, S.3    Yamazaki, M.4    Usukura, J.5    Hayashi, F.6
  • 10
    • 0034693053 scopus 로고    scopus 로고
    • Phosphorylation by cyclin-dependent protein kinase 5 of the regulatory subunit of retinal cGMP phosphodiesterase. II. Its role in the turnoff of phosphodiesterase in vivo
    • Hayashi F., Matsuura I., Kachi S., Maeda T., Yamamoto M., Fujii Y., Liu H., Yamazaki M., Usukura J., Yamazaki A. Phosphorylation by cyclin-dependent protein kinase 5 of the regulatory subunit of retinal cGMP phosphodiesterase. II. Its role in the turnoff of phosphodiesterase in vivo. J. Biol. Chem. 275:2000;32958-32965.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32958-32965
    • Hayashi, F.1    Matsuura, I.2    Kachi, S.3    Maeda, T.4    Yamamoto, M.5    Fujii, Y.6    Liu, H.7    Yamazaki, M.8    Usukura, J.9    Yamazaki, A.10
  • 11
    • 0037022535 scopus 로고    scopus 로고
    • Signal-dependent translocation of transducin, RGS9-1-Gβ5L complex, and arrestin to detergent-resistant membrane rafts in photoreceptors
    • Nair K.S., Balasubramanian N., Slepak V.Z. Signal-dependent translocation of transducin, RGS9-1-Gβ5L complex, and arrestin to detergent-resistant membrane rafts in photoreceptors. Curr. Biol. 12:2002;421-425.
    • (2002) Curr. Biol. , vol.12 , pp. 421-425
    • Nair, K.S.1    Balasubramanian, N.2    Slepak, V.Z.3
  • 12
    • 0023426241 scopus 로고
    • Fluoride complexes of aluminium or beryllium act on G-proteins as reversibly bound analogues of the γ-phosphate of GTP
    • Bigay J., Deterre P., Pfister C., Chabre M. Fluoride complexes of aluminium or beryllium act on G-proteins as reversibly bound analogues of the γ-phosphate of GTP. EMBO J. 6:1987;2907-2913.
    • (1987) EMBO J. , vol.6 , pp. 2907-2913
    • Bigay, J.1    Deterre, P.2    Pfister, C.3    Chabre, M.4
  • 13
    • 0034693139 scopus 로고    scopus 로고
    • The effector enzyme regulates the duration of G protein signaling in vertebrate photoreceptors by increasing the affinity between transducin and RGS protein
    • Skiba N.P., Hopp J.A., Arshavsky V.Y. The effector enzyme regulates the duration of G protein signaling in vertebrate photoreceptors by increasing the affinity between transducin and RGS protein. J. Biol. Chem. 275:2000;32716-32720.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32716-32720
    • Skiba, N.P.1    Hopp, J.A.2    Arshavsky, V.Y.3
  • 14
    • 0034711252 scopus 로고    scopus 로고
    • Modules in the photoreceptor RGS9-1.Gβ5L GTPase-accelerating protein complex control effector coupling, GTPase acceleration, protein folding, and stability
    • He W., Lu L., Zhang X., El-Hodiri H.M., Chen C.K., Slep K.C., Simon M.I., Jamrich M., Wensel T.G. Modules in the photoreceptor RGS9-1.Gβ5L GTPase-accelerating protein complex control effector coupling, GTPase acceleration, protein folding, and stability. J. Biol. Chem. 275:2000;37093-37100.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37093-37100
    • He, W.1    Lu, L.2    Zhang, X.3    El-Hodiri, H.M.4    Chen, C.K.5    Slep, K.C.6    Simon, M.I.7    Jamrich, M.8    Wensel, T.G.9
  • 15
    • 0022470317 scopus 로고
    • Light- and nucleotide-dependent binding of phosphodiesterase to rod disk membranes: Correlation with light-scattering changes and vesicle aggregation
    • Caretta A., Stein P.J. Light- and nucleotide-dependent binding of phosphodiesterase to rod disk membranes: correlation with light-scattering changes and vesicle aggregation. Biochemistry. 25:1986;2335-2341.
    • (1986) Biochemistry , vol.25 , pp. 2335-2341
    • Caretta, A.1    Stein, P.J.2
  • 16
    • 0029976262 scopus 로고    scopus 로고
    • A role for phospholipid polyunsaturation in modulating membrane protein function
    • Litman B.J., Mitchell D.C. A role for phospholipid polyunsaturation in modulating membrane protein function. Lipids. 31(Suppl.):1996;S193-S197.
    • (1996) Lipids , vol.31 , Issue.SUPPL.
    • Litman, B.J.1    Mitchell, D.C.2
  • 18
    • 0033747330 scopus 로고    scopus 로고
    • Cholesterol dependent recruitment of di22:6-PC by a G protein-coupled receptor into lateral domains
    • Polozova A., Litman B.J. Cholesterol dependent recruitment of di22:6-PC by a G protein-coupled receptor into lateral domains. Biophys. J. 79:2000;2632-2643.
    • (2000) Biophys. J. , vol.79 , pp. 2632-2643
    • Polozova, A.1    Litman, B.J.2
  • 19
    • 0034707082 scopus 로고    scopus 로고
    • Insolubility of lipids in Triton X-100: Physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts)
    • London E., Brown D.A. Insolubility of lipids in Triton X-100: physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts). Biochim. Biophys. Acta. 1508:2000;182-195.
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 182-195
    • London, E.1    Brown, D.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.