메뉴 건너뛰기




Volumn 19, Issue 8, 2009, Pages 700-705

Enhanced Arrestin Facilitates Recovery and Protects Rods Lacking Rhodopsin Phosphorylation (DOI:10.1016/j.cub.2009.02.065);Enhanced Arrestin Facilitates Recovery and Protects Rods Lacking Rhodopsin Phosphorylation

Author keywords

CELLBIO; SIGNALING

Indexed keywords


EID: 65049085913     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2009.04.050     Document Type: Erratum
Times cited : (65)

References (33)
  • 2
    • 0842331059 scopus 로고    scopus 로고
    • The molecular acrobatics of arrestin activation
    • Gurevich V.V., and Gurevich E.V. The molecular acrobatics of arrestin activation. Trends Pharmacol. Sci. 25 (2004) 105-111
    • (2004) Trends Pharmacol. Sci. , vol.25 , pp. 105-111
    • Gurevich, V.V.1    Gurevich, E.V.2
  • 3
    • 0027303337 scopus 로고
    • Ocular findings in a family with autosomal dominant retinitis pigmentosa and a frameshift mutation altering the carboxyl terminal sequence of rhodopsin
    • Apfelstedt-Sylla E., Kunisch M., Horn M., Ruther K., Gerding H., Gal A., and Zrenner E. Ocular findings in a family with autosomal dominant retinitis pigmentosa and a frameshift mutation altering the carboxyl terminal sequence of rhodopsin. Br. J. Ophthalmol. 77 (1993) 495-501
    • (1993) Br. J. Ophthalmol. , vol.77 , pp. 495-501
    • Apfelstedt-Sylla, E.1    Kunisch, M.2    Horn, M.3    Ruther, K.4    Gerding, H.5    Gal, A.6    Zrenner, E.7
  • 4
    • 0027487228 scopus 로고
    • Dominant retinitis pigmentosa associated with two rhodopsin gene mutations. Leu-40-Arg and an insertion disrupting the 5′-splice junction of exon 5
    • Kim R.Y., al-Maghtheh M., Fitzke F.W., Arden G.B., Jay M., Bhattacharya S.S., and Bird A.C. Dominant retinitis pigmentosa associated with two rhodopsin gene mutations. Leu-40-Arg and an insertion disrupting the 5′-splice junction of exon 5. Arch. Ophthalmol. 111 (1993) 1518-1524
    • (1993) Arch. Ophthalmol. , vol.111 , pp. 1518-1524
    • Kim, R.Y.1    al-Maghtheh, M.2    Fitzke, F.W.3    Arden, G.B.4    Jay, M.5    Bhattacharya, S.S.6    Bird, A.C.7
  • 5
    • 0027510345 scopus 로고
    • A large deletion at the 3′ end of the rhodopsin gene in an Italian family with a diffuse form of autosomal dominant retinitis pigmentosa
    • Restagno G., Maghtheh M., Bhattacharya S., Ferrone M., Garnerone S., Samuelly R., and Carbonara A. A large deletion at the 3′ end of the rhodopsin gene in an Italian family with a diffuse form of autosomal dominant retinitis pigmentosa. Hum. Mol. Genet. 2 (1993) 207-208
    • (1993) Hum. Mol. Genet. , vol.2 , pp. 207-208
    • Restagno, G.1    Maghtheh, M.2    Bhattacharya, S.3    Ferrone, M.4    Garnerone, S.5    Samuelly, R.6    Carbonara, A.7
  • 6
    • 1542290456 scopus 로고    scopus 로고
    • G proteins in cancer: The prostate cancer paradigm
    • Daaka Y. G proteins in cancer: The prostate cancer paradigm. Sci. STKE 2004 (2004) re2
    • (2004) Sci. STKE , vol.2004
    • Daaka, Y.1
  • 8
    • 0033548433 scopus 로고    scopus 로고
    • Targeted construction of phosphorylation-independent b-arrestin mutants with constitutive activity in cells
    • Kovoor A., Celver J., Abdryashitov R.I., Chavkin C., and Gurevich V.V. Targeted construction of phosphorylation-independent b-arrestin mutants with constitutive activity in cells. J. Biol. Chem. 274 (1999) 6831-6834
    • (1999) J. Biol. Chem. , vol.274 , pp. 6831-6834
    • Kovoor, A.1    Celver, J.2    Abdryashitov, R.I.3    Chavkin, C.4    Gurevich, V.V.5
  • 9
    • 0037088679 scopus 로고    scopus 로고
    • Conservation of the phosphate-sensitive elements in the arrestin family of proteins
    • Celver J., Vishnivetskiy S.A., Chavkin C., and Gurevich V.V. Conservation of the phosphate-sensitive elements in the arrestin family of proteins. J. Biol. Chem. 277 (2002) 9043-9048
    • (2002) J. Biol. Chem. , vol.277 , pp. 9043-9048
    • Celver, J.1    Vishnivetskiy, S.A.2    Chavkin, C.3    Gurevich, V.V.4
  • 11
    • 0018333003 scopus 로고
    • Responses of retinal rods to single photons
    • Baylor D.A., Lamb T.D., and Yau K.W. Responses of retinal rods to single photons. J. Physiol. 288 (1979) 613-634
    • (1979) J. Physiol. , vol.288 , pp. 613-634
    • Baylor, D.A.1    Lamb, T.D.2    Yau, K.W.3
  • 12
    • 0034731304 scopus 로고    scopus 로고
    • An additional phosphate-binding element in arrestin molecule: Implications for the mechanism of arrestin activation
    • Vishnivetskiy S.A., Schubert C., Climaco G.C., Gurevich Y.V., Velez M.-G., and Gurevich V.V. An additional phosphate-binding element in arrestin molecule: Implications for the mechanism of arrestin activation. J. Biol. Chem. 275 (2000) 41049-41057
    • (2000) J. Biol. Chem. , vol.275 , pp. 41049-41057
    • Vishnivetskiy, S.A.1    Schubert, C.2    Climaco, G.C.3    Gurevich, Y.V.4    Velez, M.-G.5    Gurevich, V.V.6
  • 14
    • 0030842611 scopus 로고    scopus 로고
    • Prolonged photoresponses in transgenic mouse rods lacking arrestin
    • Xu J., Dodd R.L., Makino C.L., Simon M.I., Baylor D.A., and Chen J. Prolonged photoresponses in transgenic mouse rods lacking arrestin. Nature 389 (1997) 505-509
    • (1997) Nature , vol.389 , pp. 505-509
    • Xu, J.1    Dodd, R.L.2    Makino, C.L.3    Simon, M.I.4    Baylor, D.A.5    Chen, J.6
  • 15
    • 27644548928 scopus 로고    scopus 로고
    • Beyond counting photons: Trials and trends in vertebrate visual transduction
    • Burns M.E., and Arshavsky V.Y. Beyond counting photons: Trials and trends in vertebrate visual transduction. Neuron 48 (2005) 387-401
    • (2005) Neuron , vol.48 , pp. 387-401
    • Burns, M.E.1    Arshavsky, V.Y.2
  • 16
    • 0033638108 scopus 로고    scopus 로고
    • Rapid and reproducible deactivation of rhodopsin requires multiple phosphorylation sites
    • Mendez A., Burns M.E., Roca A., Lem J., Wu L.W., Simon M.I., Baylor D.A., and Chen J. Rapid and reproducible deactivation of rhodopsin requires multiple phosphorylation sites. Neuron 28 (2000) 153-164
    • (2000) Neuron , vol.28 , pp. 153-164
    • Mendez, A.1    Burns, M.E.2    Roca, A.3    Lem, J.4    Wu, L.W.5    Simon, M.I.6    Baylor, D.A.7    Chen, J.8
  • 17
    • 33746659395 scopus 로고    scopus 로고
    • Multiple phosphorylation sites confer reproducibility of the rod's single-photon responses
    • Doan T., Mendez A., Detwiler P.B., Chen J., and Rieke F. Multiple phosphorylation sites confer reproducibility of the rod's single-photon responses. Science 313 (2006) 530-533
    • (2006) Science , vol.313 , pp. 530-533
    • Doan, T.1    Mendez, A.2    Detwiler, P.B.3    Chen, J.4    Rieke, F.5
  • 19
    • 0030050756 scopus 로고    scopus 로고
    • Recovery phase of the murine rod photoresponse reconstructed from electroretinographic recordings
    • Lyubarsky A.L., and Pugh Jr. E.N. Recovery phase of the murine rod photoresponse reconstructed from electroretinographic recordings. J. Neurosci. 16 (1996) 563-571
    • (1996) J. Neurosci. , vol.16 , pp. 563-571
    • Lyubarsky, A.L.1    Pugh Jr., E.N.2
  • 20
    • 0029360356 scopus 로고
    • Response linearity and kinetics of the cat retina: The bipolar cell component of the dark-adapted electroretinogram
    • Robson J.G., and Frishman L.J. Response linearity and kinetics of the cat retina: The bipolar cell component of the dark-adapted electroretinogram. Vis. Neurosci. 12 (1995) 837-850
    • (1995) Vis. Neurosci. , vol.12 , pp. 837-850
    • Robson, J.G.1    Frishman, L.J.2
  • 21
    • 0032323525 scopus 로고    scopus 로고
    • Dissecting the dark-adapted electroretinogram
    • Robson J.G., and Frishman L.J. Dissecting the dark-adapted electroretinogram. Doc. Ophthalmol. 95 (1999) 187-215
    • (1999) Doc. Ophthalmol. , vol.95 , pp. 187-215
    • Robson, J.G.1    Frishman, L.J.2
  • 22
    • 0002241584 scopus 로고    scopus 로고
    • The origin of the major rod- and cone-driven components of the rodent electroretinogram, and the effect of age and light-rearing history on the magnitudes of these components
    • Williams T.P., and Thistle A.B. (Eds), Plenum Press, New York
    • Pugh Jr. E.N., Falsini B., and Lyubarsky A.L. The origin of the major rod- and cone-driven components of the rodent electroretinogram, and the effect of age and light-rearing history on the magnitudes of these components. In: Williams T.P., and Thistle A.B. (Eds). Photostasis and Related Phenomena (1998), Plenum Press, New York 93-128
    • (1998) Photostasis and Related Phenomena , pp. 93-128
    • Pugh Jr., E.N.1    Falsini, B.2    Lyubarsky, A.L.3
  • 23
    • 0030868289 scopus 로고    scopus 로고
    • Photoresponses of human rods in vivo derived from paired-flash electroretinograms
    • Pepperberg D.R., Birch D.G., and Hood D.C. Photoresponses of human rods in vivo derived from paired-flash electroretinograms. Vis. Neurosci. 14 (1997) 73-82
    • (1997) Vis. Neurosci. , vol.14 , pp. 73-82
    • Pepperberg, D.R.1    Birch, D.G.2    Hood, D.C.3
  • 24
    • 0028955343 scopus 로고
    • Mechanisms of rhodopsin inactivation in vivo as revealed by a COOH-terminal truncation mutant
    • Chen J., Makino C.L., Peachey N.S., Baylor D.A., and Simon M.I. Mechanisms of rhodopsin inactivation in vivo as revealed by a COOH-terminal truncation mutant. Science 267 (1995) 374-377
    • (1995) Science , vol.267 , pp. 374-377
    • Chen, J.1    Makino, C.L.2    Peachey, N.S.3    Baylor, D.A.4    Simon, M.I.5
  • 25
    • 0027241013 scopus 로고
    • Visual arrestin interaction with rhodopsin. Sequential multisite binding ensures strict selectivity towards light-activated phosphorylated rhodopsin
    • Gurevich V.V., and Benovic J.L. Visual arrestin interaction with rhodopsin. Sequential multisite binding ensures strict selectivity towards light-activated phosphorylated rhodopsin. J. Biol. Chem. 268 (1993) 11628-11638
    • (1993) J. Biol. Chem. , vol.268 , pp. 11628-11638
    • Gurevich, V.V.1    Benovic, J.L.2
  • 27
    • 0347723912 scopus 로고    scopus 로고
    • Mapping the arrestin-receptor interface: Structural elements responsible for receptor specificity of arrestin proteins
    • Vishnivetskiy S.A., Hosey M.M., Benovic J.L., and Gurevich V.V. Mapping the arrestin-receptor interface: Structural elements responsible for receptor specificity of arrestin proteins. J. Biol. Chem. 279 (2004) 1262-1268
    • (2004) J. Biol. Chem. , vol.279 , pp. 1262-1268
    • Vishnivetskiy, S.A.1    Hosey, M.M.2    Benovic, J.L.3    Gurevich, V.V.4
  • 28
    • 0028924619 scopus 로고
    • Visual arrestin binding to rhodopsin: Diverse functional roles of positively charged residues within the phosphorylation-recignition region of arrestin
    • Gurevich V.V., and Benovic J.L. Visual arrestin binding to rhodopsin: Diverse functional roles of positively charged residues within the phosphorylation-recignition region of arrestin. J. Biol. Chem. 270 (1995) 6010-6016
    • (1995) J. Biol. Chem. , vol.270 , pp. 6010-6016
    • Gurevich, V.V.1    Benovic, J.L.2
  • 29
    • 33645524290 scopus 로고    scopus 로고
    • The differential engagement of arrestin surface charges by the various functional forms of the receptor
    • Hanson S.M., and Gurevich V.V. The differential engagement of arrestin surface charges by the various functional forms of the receptor. J. Biol. Chem. 281 (2006) 3458-3462
    • (2006) J. Biol. Chem. , vol.281 , pp. 3458-3462
    • Hanson, S.M.1    Gurevich, V.V.2
  • 31
    • 0029067542 scopus 로고
    • A homozygous 1-base pair deletion in the arrestin gene is a frequent cause of Oguchi disease in Japanese
    • Fuchs S., Nakazawa M., Maw M., Tamai M., Oguchi Y., and Gal A. A homozygous 1-base pair deletion in the arrestin gene is a frequent cause of Oguchi disease in Japanese. Nat. Genet. 10 (1995) 360-362
    • (1995) Nat. Genet. , vol.10 , pp. 360-362
    • Fuchs, S.1    Nakazawa, M.2    Maw, M.3    Tamai, M.4    Oguchi, Y.5    Gal, A.6
  • 32
    • 0031038950 scopus 로고    scopus 로고
    • Defects in the rhodopsin kinase gene in the Oguchi form of stationary night blindness
    • Yamamoto S., Sippel K.C., Berson E.L., and Dryja T.P. Defects in the rhodopsin kinase gene in the Oguchi form of stationary night blindness. Nat. Genet. 15 (1997) 175-178
    • (1997) Nat. Genet. , vol.15 , pp. 175-178
    • Yamamoto, S.1    Sippel, K.C.2    Berson, E.L.3    Dryja, T.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.