메뉴 건너뛰기




Volumn 349, Issue 1, 2006, Pages 345-352

Corrigendum to "Ca2+/recoverin dependent regulation of phosphorylation of the rhodopsin mutant R135L associated with retinitis pigmentosa" [Biochem. Biophys. Res. Commun. 349 (2006) 345-352] (DOI:10.1016/j.bbrc.2006.08.048);Ca2+/recoverin dependent regulation of phosphorylation of the rhodopsin mutant R135L associated with retinitis pigmentosa

Author keywords

Calcium; Recoverin; Retinitis pigmentosa; Rhodopsin kinase; Rhodopsin mutation; Rhodopsin phosphorylation; Transducin activation; Visual phototransduction

Indexed keywords

CALCIUM; GUANINE NUCLEOTIDE BINDING PROTEIN; RECOVERIN; RHODOPSIN; RHODOPSIN KINASE; TRANSDUCIN;

EID: 33748317961     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.09.050     Document Type: Erratum
Times cited : (11)

References (49)
  • 1
    • 0037095736 scopus 로고    scopus 로고
    • Retinitis pigmentosa and allied diseases: numerous diseases, genes, and inheritance patterns
    • Rivolta C., Sharon D., DeAngelis M.M., and Dryja T.P. Retinitis pigmentosa and allied diseases: numerous diseases, genes, and inheritance patterns. Hum. Mol. Genet. 11 (2002) 1219-1227
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1219-1227
    • Rivolta, C.1    Sharon, D.2    DeAngelis, M.M.3    Dryja, T.P.4
  • 4
    • 0026058548 scopus 로고
    • Functional heterogeneity of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa
    • Sung C.H., Schneider B.G., Agarwal N., Papermaster D.S., and Nathans J. Functional heterogeneity of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa. Proc. Natl. Acad. Sci. USA 88 (1991) 8840-8844
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8840-8844
    • Sung, C.H.1    Schneider, B.G.2    Agarwal, N.3    Papermaster, D.S.4    Nathans, J.5
  • 5
    • 0025306687 scopus 로고
    • Role of the intradiscal domain in rhodopsin assembly and function
    • Doi T., Molday R.S., and Khorana H.G. Role of the intradiscal domain in rhodopsin assembly and function. Proc. Natl. Acad. Sci. USA 87 (1990) 4991-4995
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4991-4995
    • Doi, T.1    Molday, R.S.2    Khorana, H.G.3
  • 6
    • 0028287273 scopus 로고
    • Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa
    • Kaushal S., and Khorana H.G. Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa. Biochemistry 33 (1994) 6121-6128
    • (1994) Biochemistry , vol.33 , pp. 6121-6128
    • Kaushal, S.1    Khorana, H.G.2
  • 7
    • 9444283151 scopus 로고    scopus 로고
    • Molecular biology of retinitis pigmentosa: therapeutic implications
    • Ramon E., del Valle L.J., and Garriga P. Molecular biology of retinitis pigmentosa: therapeutic implications. Curr. Pharmacogenomics 2 (2004) 339-349
    • (2004) Curr. Pharmacogenomics , vol.2 , pp. 339-349
    • Ramon, E.1    del Valle, L.J.2    Garriga, P.3
  • 8
    • 0037470723 scopus 로고    scopus 로고
    • Altered functionality in rhodopsin point mutants associated with retinitis pigmentosa
    • Andres A., Garriga P., and Manyosa J. Altered functionality in rhodopsin point mutants associated with retinitis pigmentosa. Biochem. Biophys. Res. Commun. 303 (2003) 294-301
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , pp. 294-301
    • Andres, A.1    Garriga, P.2    Manyosa, J.3
  • 9
    • 0038482177 scopus 로고    scopus 로고
    • Structural and functional role of helices I and II in rhodopsin. A novel interplay evidenced by mutations at Gly-51 and Gly-89 in the transmembrane domain
    • Bosch L., Ramon E., del Valle L.J., and Garriga P. Structural and functional role of helices I and II in rhodopsin. A novel interplay evidenced by mutations at Gly-51 and Gly-89 in the transmembrane domain. J. Biol. Chem. 278 (2003) 20203-20209
    • (2003) J. Biol. Chem. , vol.278 , pp. 20203-20209
    • Bosch, L.1    Ramon, E.2    del Valle, L.J.3    Garriga, P.4
  • 10
    • 0037458628 scopus 로고    scopus 로고
    • Unusual thermal and conformational properties of the rhodopsin congenital night blindness mutant Thr-94 → Ile
    • Ramon E., del Valle J.L., and Garriga P. Unusual thermal and conformational properties of the rhodopsin congenital night blindness mutant Thr-94 → Ile. J. Biol. Chem. 278 (2003) 6427-6432
    • (2003) J. Biol. Chem. , vol.278 , pp. 6427-6432
    • Ramon, E.1    del Valle, J.L.2    Garriga, P.3
  • 12
    • 0020713543 scopus 로고
    • Monoclonal antibodies to rhodopsin: characterization, cross-reactivity, and application as structural probes
    • Molday R.S., and MacKenzie D. Monoclonal antibodies to rhodopsin: characterization, cross-reactivity, and application as structural probes. Biochemistry 22 (1983) 653-660
    • (1983) Biochemistry , vol.22 , pp. 653-660
    • Molday, R.S.1    MacKenzie, D.2
  • 13
    • 2442606621 scopus 로고    scopus 로고
    • The spectrum of human rhodopsin disease mutations through the lens of interspecific variation
    • Briscoe A.D., Gaur C., and Kumar S. The spectrum of human rhodopsin disease mutations through the lens of interspecific variation. Gene 332 (2004) 107-118
    • (2004) Gene , vol.332 , pp. 107-118
    • Briscoe, A.D.1    Gaur, C.2    Kumar, S.3
  • 14
    • 17044363529 scopus 로고    scopus 로고
    • Mechanisms of cell death in rhodopsin retinitis pigmentosa: implications for therapy
    • Mendes H.F., van der Spuy J., Chapple J.P., and Cheetham M.E. Mechanisms of cell death in rhodopsin retinitis pigmentosa: implications for therapy. Trends Mol. Med. 11 (2005) 177-185
    • (2005) Trends Mol. Med. , vol.11 , pp. 177-185
    • Mendes, H.F.1    van der Spuy, J.2    Chapple, J.P.3    Cheetham, M.E.4
  • 15
    • 0029944275 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: correct folding and misfolding in point mutants at and in proximity to the site of the retinitis pigmentosa mutation Leu-125 → Arg in the transmembrane helix C
    • Garriga P., Liu X., and Khorana H.G. Structure and function in rhodopsin: correct folding and misfolding in point mutants at and in proximity to the site of the retinitis pigmentosa mutation Leu-125 → Arg in the transmembrane helix C. Proc. Natl. Acad. Sci. USA 93 (1996) 4560-4564
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4560-4564
    • Garriga, P.1    Liu, X.2    Khorana, H.G.3
  • 16
    • 0029943263 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: correct folding and misfolding in two point mutants in the intradiscal domain of rhodopsin identified in retinitis pigmentosa
    • Liu X., Garriga P., and Khorana H.G. Structure and function in rhodopsin: correct folding and misfolding in two point mutants in the intradiscal domain of rhodopsin identified in retinitis pigmentosa. Proc. Natl. Acad. Sci. USA 93 (1996) 4554-4559
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4554-4559
    • Liu, X.1    Garriga, P.2    Khorana, H.G.3
  • 17
    • 0033515036 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function
    • Hwa J., Reeves P.J., Klein-Seetharaman J., Davidson F., and Khorana H.G. Structure and function in rhodopsin: further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function. Proc. Natl. Acad. Sci. USA 96 (1999) 1932-1935
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1932-1935
    • Hwa, J.1    Reeves, P.J.2    Klein-Seetharaman, J.3    Davidson, F.4    Khorana, H.G.5
  • 18
    • 12544250742 scopus 로고    scopus 로고
    • Suppression of wild-type rhodopsin maturation by mutants linked to autosomal dominant retinitis pigmentosa
    • Rajan R.S., and Kopito R.R. Suppression of wild-type rhodopsin maturation by mutants linked to autosomal dominant retinitis pigmentosa. J. Biol. Chem. 280 (2005) 1284-1291
    • (2005) J. Biol. Chem. , vol.280 , pp. 1284-1291
    • Rajan, R.S.1    Kopito, R.R.2
  • 19
    • 1642603437 scopus 로고    scopus 로고
    • Constitutive opsin signaling: night blindness or retinal degeneration?
    • Lem J., and Fain G.L. Constitutive opsin signaling: night blindness or retinal degeneration?. Trends Mol. Med. 10 (2004) 150-157
    • (2004) Trends Mol. Med. , vol.10 , pp. 150-157
    • Lem, J.1    Fain, G.L.2
  • 20
    • 0037117560 scopus 로고    scopus 로고
    • Activation of mislocalized opsin kills rod cells: a novel mechanism for rod cell death in retinal disease
    • Alfinito P.D., and Townes-Anderson E. Activation of mislocalized opsin kills rod cells: a novel mechanism for rod cell death in retinal disease. Proc. Natl. Acad. Sci. USA 99 (2002) 5655-5660
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5655-5660
    • Alfinito, P.D.1    Townes-Anderson, E.2
  • 21
    • 30644475101 scopus 로고    scopus 로고
    • Mislocalized rhodopsin does not require activation to cause retinal degeneration and neurite outgrowth in Xenopus laevis
    • Tam B.M., Xie G., Oprian D.D., and Moritz O.L. Mislocalized rhodopsin does not require activation to cause retinal degeneration and neurite outgrowth in Xenopus laevis. J. Neurosci. 26 (2006) 203-209
    • (2006) J. Neurosci. , vol.26 , pp. 203-209
    • Tam, B.M.1    Xie, G.2    Oprian, D.D.3    Moritz, O.L.4
  • 22
    • 33645836308 scopus 로고    scopus 로고
    • Why photoreceptors die (and why they don't)
    • Fain G.L. Why photoreceptors die (and why they don't). Bioessays 28 (2006) 344-354
    • (2006) Bioessays , vol.28 , pp. 344-354
    • Fain, G.L.1
  • 23
    • 33645535034 scopus 로고    scopus 로고
    • G protein-coupled receptor rhodopsin
    • Palczewski K. G protein-coupled receptor rhodopsin. Annu. Rev. Biochem. 75 (2006) 743-767
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 743-767
    • Palczewski, K.1
  • 26
    • 0032492650 scopus 로고    scopus 로고
    • Rhodopsin arginine-135 mutants are phosphorylated by rhodopsin kinase and bind arrestin in the absence of 11-cis-retinal
    • Shi W., Sports C.D., Raman D., Shirakawa S., Osawa S., and Weiss E.R. Rhodopsin arginine-135 mutants are phosphorylated by rhodopsin kinase and bind arrestin in the absence of 11-cis-retinal. Biochemistry 37 (1998) 4869-4874
    • (1998) Biochemistry , vol.37 , pp. 4869-4874
    • Shi, W.1    Sports, C.D.2    Raman, D.3    Shirakawa, S.4    Osawa, S.5    Weiss, E.R.6
  • 27
    • 0030950010 scopus 로고    scopus 로고
    • Autosomal dominant retinitis pigmentosa with a rhodopsin mutation (Arg-135-Trp). Disease phenotype in a Swedish family
    • Ponjavic V., Abrahamson M., Andreasson S., Ehinger B., and Fex G. Autosomal dominant retinitis pigmentosa with a rhodopsin mutation (Arg-135-Trp). Disease phenotype in a Swedish family. Acta Ophthalmol. Scand. 75 (1997) 218-223
    • (1997) Acta Ophthalmol. Scand. , vol.75 , pp. 218-223
    • Ponjavic, V.1    Abrahamson, M.2    Andreasson, S.3    Ehinger, B.4    Fex, G.5
  • 28
    • 0029828733 scopus 로고    scopus 로고
    • Autosomal-dominant retinitis pigmentosa associated with an Arg-135-Trp point mutation of the rhodopsin gene. Clinical features and longitudinal observations
    • Pannarale M.R., Grammatico B., Iannaccone A., Forte R., DeBernardo C., Flagiello L., Vingolo E.M., and Del Porto G. Autosomal-dominant retinitis pigmentosa associated with an Arg-135-Trp point mutation of the rhodopsin gene. Clinical features and longitudinal observations. Ophthalmology 103 (1996) 1443-1452
    • (1996) Ophthalmology , vol.103 , pp. 1443-1452
    • Pannarale, M.R.1    Grammatico, B.2    Iannaccone, A.3    Forte, R.4    DeBernardo, C.5    Flagiello, L.6    Vingolo, E.M.7    Del Porto, G.8
  • 29
    • 84907115076 scopus 로고
    • A six-generation family with autosomal dominant retinitis pigmentosa and a rhodopsin gene mutation (arginine-135-leucine)
    • Andreasson S., Ehinger B., Abrahamson M., and Fex G. A six-generation family with autosomal dominant retinitis pigmentosa and a rhodopsin gene mutation (arginine-135-leucine). Ophthalmic. Paediatr. Genet. 13 (1992) 145-153
    • (1992) Ophthalmic. Paediatr. Genet. , vol.13 , pp. 145-153
    • Andreasson, S.1    Ehinger, B.2    Abrahamson, M.3    Fex, G.4
  • 31
    • 3242778617 scopus 로고    scopus 로고
    • Structural and functional impairment of endocytic pathways by retinitis pigmentosa mutant rhodopsin-arrestin complexes
    • Chuang J.Z., Vega C., Jun W., and Sung C.H. Structural and functional impairment of endocytic pathways by retinitis pigmentosa mutant rhodopsin-arrestin complexes. J. Clin. Invest. 114 (2004) 131-140
    • (2004) J. Clin. Invest. , vol.114 , pp. 131-140
    • Chuang, J.Z.1    Vega, C.2    Jun, W.3    Sung, C.H.4
  • 32
    • 0028363788 scopus 로고
    • A new locus for autosomal dominant retinitis pigmentosa on the short arm of chromosome 17
    • Greenberg J., Goliath R., Beighton P., and Ramesar R. A new locus for autosomal dominant retinitis pigmentosa on the short arm of chromosome 17. Hum. Mol. Genet. 3 (1994) 915-918
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 915-918
    • Greenberg, J.1    Goliath, R.2    Beighton, P.3    Ramesar, R.4
  • 34
    • 0030989004 scopus 로고    scopus 로고
    • Evaluation of the human gene encoding recoverin in patients with retinitis pigmentosa or an allied disease
    • Parminder A.H., Murakami A., Inana G., Berson E.L., and Dryja T.P. Evaluation of the human gene encoding recoverin in patients with retinitis pigmentosa or an allied disease. Invest. Ophthalmol. Vis. Sci. 38 (1997) 704-709
    • (1997) Invest. Ophthalmol. Vis. Sci. , vol.38 , pp. 704-709
    • Parminder, A.H.1    Murakami, A.2    Inana, G.3    Berson, E.L.4    Dryja, T.P.5
  • 35
    • 0036986605 scopus 로고    scopus 로고
    • Pathological roles of recoverin in cancer-associated retinopathy
    • Ohguro H., and Nakazawa M. Pathological roles of recoverin in cancer-associated retinopathy. Adv. Exp. Med. Biol. 514 (2002) 109-124
    • (2002) Adv. Exp. Med. Biol. , vol.514 , pp. 109-124
    • Ohguro, H.1    Nakazawa, M.2
  • 38
    • 0027715151 scopus 로고
    • Interaction between photoactivated rhodopsin and its kinase: stability and kinetics of complex formation
    • Pulvermüller A., Palczewski K., and Hofmann K.P. Interaction between photoactivated rhodopsin and its kinase: stability and kinetics of complex formation. Biochemistry 32 (1993) 14082-14088
    • (1993) Biochemistry , vol.32 , pp. 14082-14088
    • Pulvermüller, A.1    Palczewski, K.2    Hofmann, K.P.3
  • 39
    • 0031015901 scopus 로고    scopus 로고
    • Recoverin inhibits the phosphorylation of dark-adapted rhodopsin more than it does that of bleached rhodopsin: a possible mechanism through which rhodopsin kinase is prevented from participation in a side reaction
    • Senin I.I., Dean K.R., Zargarov A.A., Akhtar M., and Philippov P.P. Recoverin inhibits the phosphorylation of dark-adapted rhodopsin more than it does that of bleached rhodopsin: a possible mechanism through which rhodopsin kinase is prevented from participation in a side reaction. Biochem. J. 321 (1997) 551-555
    • (1997) Biochem. J. , vol.321 , pp. 551-555
    • Senin, I.I.1    Dean, K.R.2    Zargarov, A.A.3    Akhtar, M.4    Philippov, P.P.5
  • 40
    • 0018901497 scopus 로고
    • Light- and GTP-regulated interaction of GTPase and other proteins with bovine photoreceptor membranes
    • Kuhn H. Light- and GTP-regulated interaction of GTPase and other proteins with bovine photoreceptor membranes. Nature 283 (1980) 587-589
    • (1980) Nature , vol.283 , pp. 587-589
    • Kuhn, H.1
  • 41
    • 0027273840 scopus 로고
    • Characterization of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa. Mutations on the cytoplasmic surface affect transducin activation
    • Min M.C., Zvyaga T.A., Cypess A.M., and Sakmar T.P. Characterization of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa. Mutations on the cytoplasmic surface affect transducin activation. J. Biol. Chem. 268 (1993) 9400-9404
    • (1993) J. Biol. Chem. , vol.268 , pp. 9400-9404
    • Min, M.C.1    Zvyaga, T.A.2    Cypess, A.M.3    Sakmar, T.P.4
  • 42
    • 33645519597 scopus 로고    scopus 로고
    • A role for direct interactions in the modulation of rhodopsin by omega-3 polyunsaturated lipids
    • Grossfield A., Feller S.E., and Pitman M.C. A role for direct interactions in the modulation of rhodopsin by omega-3 polyunsaturated lipids. Proc. Natl. Acad. Sci. USA 103 (2006) 4888-4893
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 4888-4893
    • Grossfield, A.1    Feller, S.E.2    Pitman, M.C.3
  • 44
    • 12344265692 scopus 로고    scopus 로고
    • Environmental light and heredity are associated with adaptive changes in retinal DHA levels that affect retinal function
    • Anderson R.E., and Penn J.S. Environmental light and heredity are associated with adaptive changes in retinal DHA levels that affect retinal function. Lipids 39 (2004) 1121-1124
    • (2004) Lipids , vol.39 , pp. 1121-1124
    • Anderson, R.E.1    Penn, J.S.2
  • 45
    • 23044483866 scopus 로고    scopus 로고
    • Properties of docosahexaenoic-acid-containing lipids and their influence on the function of rhodopsin
    • Feller S.E., and Gawrisch K. Properties of docosahexaenoic-acid-containing lipids and their influence on the function of rhodopsin. Curr. Opin. Struct. Biol. 15 (2005) 416-422
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 416-422
    • Feller, S.E.1    Gawrisch, K.2
  • 47
    • 0030299881 scopus 로고    scopus 로고
    • 2+! The physiology and pathology of Ca(2+)-binding proteins in the retina
    • 2+! The physiology and pathology of Ca(2+)-binding proteins in the retina. Trends Neurosci. 19 (1996) 547-554
    • (1996) Trends Neurosci. , vol.19 , pp. 547-554
    • Polans, A.1    Baehr, W.2    Palczewski, K.3
  • 49
    • 33745815637 scopus 로고    scopus 로고
    • Recoverin binds exclusively to an amphipathic peptide at the N-terminus of rhodopsin kinase, inhibiting rhodopsin phosphorylation without affecting catalytic activity of the kinase
    • Higgins M.K., Oprian D.D., and Schertler G.F. Recoverin binds exclusively to an amphipathic peptide at the N-terminus of rhodopsin kinase, inhibiting rhodopsin phosphorylation without affecting catalytic activity of the kinase. J. Biol. Chem. 281 (2006) 19426-19432
    • (2006) J. Biol. Chem. , vol.281 , pp. 19426-19432
    • Higgins, M.K.1    Oprian, D.D.2    Schertler, G.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.