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'''Rhodopsin kinase''' ({{EC number|2.7.11.14}}, ''cone opsin kinase'', ''G-protein-coupled receptor kinase 1'', ''GPCR kinase 1'', ''GRK1'', ''GRK7'', ''opsin kinase'', ''opsin kinase (phosphorylating)'', ''rhodopsin kinase (phosphorylating)'', ''RK'', ''STK14'') is a [[serine/threonine-specific protein kinase]] involved in [[phototransduction]].<ref>{{cite journal | title = The Receptor Kinase Family: Primary Structure of Rhodopsin Kinase Reveals Similarities to the &beta;-Adrenergic Receptor Kinase|author1 = Lorenz, W. |author2 = Inglese, J. |author3 = Palczewski. K.J. | author4 = Onorato, J. |author5 =Caron, M.G. |author6 =Lefkowitz, R.J. | journal = Proc. Nat’l Acad. Sci. USA |date = 1991 |volume = 88 |pages = 8715–8719 |pmid = 1656454}}</ref><ref>{{cite journal | title = Light-dependent phosphorylation of rhodopsin by &beta;-adrenergic receptor kinase |author1 = Benovic, J.L. |author2 =Mayor, F. Jr. |author3 =Somers, R.L. |author4 =Caron, M.G. |author5 =Lefkowitz, R.J. | journal = Nature |date = 1986 |volume = 321 |pages = 869–872 |pmid = 3014340 |doi=10.1038/321869a0 |issue=6073}}</ref><ref>{{cite journal | title = Light-dependent phosphorylation of rhodopsin. Purification and properties of rhodopsin kinase |author1 = Shichi, H. |author2 =Somers, R.L. |journal = J. Biol. Chem. |date = 1978 |volume = 253 |pages = 7040–7046 |pmid = 690139 |issue=19}}</ref><ref>{{cite journal | title = Purification and characterization of rhodopsin kinase |author1 = Palczewski, K. |author2 =McDowell, J.H. |author3 =Hargrave, P.A. |journal = J. Biol. Chem. |date = 1988 |volume = 263 |pages = 14067–14073 |pmid = 2844754 |issue=28}}</ref><ref>{{cite journal | title = Light-stimulated phosphorylation of rhodopsin in the retina: the presence of a protein kinase that is specific for photobleached rhodopsin |author1 = Weller, M. |author2 =Virmaux, N. |author3 =Mandel, P. |journal = Proc. Natl. Acad. Sci. USA |date = 1975 |volume = 72 |pages = 381–385 |pmid = 164024 |issue=1 |doi=10.1073/pnas.72.1.381 |pmc=432309}}</ref><ref>{{cite journal | title = Rhodopsin kinase: expression in baculovirus-infected insect cells, and characterization of post-translational modifications |author1 = Cha, K. |author2 =Bruel, C. |author3 =Inglese, J. |author4 =Khorana, H.G. |journal = Proc. Natl. Acad. Sci. USA |date = 1997 |volume = 94 |pages = 10577–10582 |pmid = 9380677 |issue=20 |doi=10.1073/pnas.94.20.10577 |pmc=23407}}</ref><ref>{{cite journal | title = Characterization and chromosomal localization of the gene for human rhodopsin kinase |author1 = Khani, S.C. |author2 =Abitbol, M. |author3 =Yamamoto, S. |author4 =Maravic-Magovcevic, I. |author5 =Dryja, T.P. |journal = Genomics |date = 1996 |volume = 35 |pages = 571–576 |pmid = 8812493 |doi=10.1006/geno.1996.0399 |issue=3}}</ref><ref>{{cite journal | title = Characterization of human GRK7 as a potential cone opsin kinase |author1 = Chen, C.K. |author2 =Zhang, K. |author3 =Church-Kopish, J. |author4 =Huang, W. |author5 =Zhang, H. |author6 =Chen, Y.J. |author7 =Frederick, J.M. |author8 =Baehr, W. | journal = Mol. Vis. |date = 2001 |volume = 7 |pages = 305–313 |pmid = 11754336}}</ref><ref>{{cite journal | title = Non-visual GRKs: are we seeing the whole picture? |author1 = Willets, J.M. |author2 =Challiss, R.A. |author3 =Nahorski, S.R. |journal = Trends Pharmacol. Sci. |date = 2003 |volume = 24 |pages = 626–633 |pmid = 14654303 |doi=10.1016/j.tips.2003.10.003}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]
'''Rhodopsin kinase''' ({{EC number|2.7.11.14}}, ''cone opsin kinase'', ''G-protein-coupled receptor kinase 1'', ''GPCR kinase 1'', ''GRK1'', ''GRK7'', ''opsin kinase'', ''opsin kinase (phosphorylating)'', ''rhodopsin kinase (phosphorylating)'', ''RK'', ''STK14'') is a [[serine/threonine-specific protein kinase]] involved in [[phototransduction]].<ref>{{cite journal | vauthors = Lorenz W, Inglese J, Palczewski K, Onorato JJ, Caron MG, Lefkowitz RJ | title = The receptor kinase family: primary structure of rhodopsin kinase reveals similarities to the beta-adrenergic receptor kinase | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 88 | issue = 19 | pages = 8715–9 | date = October 1991 | pmid = 1656454 | doi=10.1073/pnas.88.19.8715 | pmc=52580}}</ref><ref>{{cite journal | vauthors = Benovic JL, Mayor F, Somers RL, Caron MG, Lefkowitz RJ | title = Light-dependent phosphorylation of rhodopsin by beta-adrenergic receptor kinase | journal = Nature | volume = 321 | issue = 6073 | pages = 869–72 | date = 1986 | pmid = 3014340 | doi = 10.1038/321869a0 }}</ref><ref>{{cite journal | vauthors = Shichi H, Somers RL | title = Light-dependent phosphorylation of rhodopsin. Purification and properties of rhodopsin kinase | journal = The Journal of Biological Chemistry | volume = 253 | issue = 19 | pages = 7040–6 | date = October 1978 | pmid = 690139 }}</ref><ref>{{cite journal | vauthors = Palczewski K, McDowell JH, Hargrave PA | title = Purification and characterization of rhodopsin kinase | journal = The Journal of Biological Chemistry | volume = 263 | issue = 28 | pages = 14067–73 | date = October 1988 | pmid = 2844754 }}</ref><ref>{{cite journal | vauthors = Weller M, Virmaux N, Mandel P | title = Light-stimulated phosphorylation of rhodopsin in the retina: the presence of a protein kinase that is specific for photobleached rhodopsin | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 72 | issue = 1 | pages = 381–5 | date = January 1975 | pmid = 164024 | pmc = 432309 | doi = 10.1073/pnas.72.1.381 }}</ref><ref>{{cite journal | vauthors = Cha K, Bruel C, Inglese J, Khorana HG | title = Rhodopsin kinase: expression in baculovirus-infected insect cells, and characterization of post-translational modifications | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 94 | issue = 20 | pages = 10577–82 | date = September 1997 | pmid = 9380677 | pmc = 23407 | doi = 10.1073/pnas.94.20.10577 }}</ref><ref>{{cite journal | vauthors = Khani SC, Abitbol M, Yamamoto S, Maravic-Magovcevic I, Dryja TP | title = Characterization and chromosomal localization of the gene for human rhodopsin kinase | journal = Genomics | volume = 35 | issue = 3 | pages = 571–6 | date = August 1996 | pmid = 8812493 | doi = 10.1006/geno.1996.0399 }}</ref><ref>{{cite journal | vauthors = Chen CK, Zhang K, Church-Kopish J, Huang W, Zhang H, Chen YJ, Frederick JM, Baehr W | title = Characterization of human GRK7 as a potential cone opsin kinase | journal = Molecular Vision | volume = 7 | pages = 305–13 | date = December 2001 | pmid = 11754336 }}</ref><ref>{{cite journal | vauthors = Willets JM, Challiss RA, Nahorski SR | title = Non-visual GRKs: are we seeing the whole picture? | journal = Trends in Pharmacological Sciences | volume = 24 | issue = 12 | pages = 626–33 | date = December 2003 | pmid = 14654303 | doi = 10.1016/j.tips.2003.10.003 }}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]


: ATP + [[rhodopsin]] <math>\rightleftharpoons</math> ADP + [[phosphorhodopsin]]
: ATP + [[rhodopsin]] <math>\rightleftharpoons</math> ADP + [[phosphorhodopsin]]


Mutations in rhodopsin kinase are associated with a form of night blindness called [[Oguchi disease]].<ref>{{cite journal | title = Defects in the rhodopsin kinase gene in the Oguchi form of stationary night blindness. |vauthors = Yamamoto S, Sippel KC, Berson EL, Dryja TP |journal = Nat. Genet. |date = 1997 |volume = 15 |pages = 175–8 |pmid = 9020843 |issue=2 |doi=10.1038/ng0297-175}}</ref>
Mutations in rhodopsin kinase are associated with a form of night blindness called [[Oguchi disease]].<ref>{{cite journal | vauthors = Yamamoto S, Sippel KC, Berson EL, Dryja TP | title = Defects in the rhodopsin kinase gene in the Oguchi form of stationary night blindness | journal = Nature Genetics | volume = 15 | issue = 2 | pages = 175–8 | date = February 1997 | pmid = 9020843 | doi = 10.1038/ng0297-175 }}</ref>


==More on Rhodopsin Kinase==
==More on Rhodopsin Kinase==
Rhodopsin Kinase is involved in mammalian rod cells specifically with photo transduction and belongs to the family of G coupled-protein receptor kinases. This kinase, referred to as GRK1 is post-translationally modified by farnesylation and &alpha;-carboxyl methylation<ref>{{cite journal | title = Isoprenylation of a Protein Kinase: Farnesylation / &alpha;-Carboxyl Methylation Required for Full Enzymatic Activity of Rhodopsin Kinase. |author1 = Inglese, J. |author2 = Glickman, J.F. |author3 = Lorenz, W. | author4 =Caron, M.G. |author5 =Lefkowitz, R.J. | journal = J. Biol. Chem.|date = 1992 |volume = 267|pages = 1422–1425|pmid = 1730692 }}</ref><ref name="kutuzov">{{cite journal|last1=Kutuzov|first1=Mikhail A.|last2=Andreeva|first2=Alexandra V.|last3=Bennett|first3=Nelly|title=Regulation of the methylation status of G protein-coupled receptor kinase 1 (rhodopsin kinase)|journal=Cellular Signalling|date=December 2012|volume=24|issue=12|pages=2259–2267|doi=10.1016/j.cellsig.2012.07.020|accessdate=7 November 2016}}</ref> GRK1 phosphorylates rhodopsin, resulting in partial photo-activation of rhodopsin, thus activating the dim flash response.<ref name="sakurai">{{cite journal|last1=Sakurai|first1=Keisuke|last2=Chen|first2=Jeannie|last3=Khani|first3=Shahrokh C.|last4=Kefalov|first4=Vladimir J.|title=Regulation of Mammalian Cone Phototransduction by Recoverin and Rhodopsin Kinase|journal=Journal of Biological Chemistry|date=3 April 2015|volume=290|issue=14|pages=9239–9250|doi=10.1074/jbc.M115.639591|pmid=25673692|pmc=4423708}}</ref> Dim flash response is activated in dim light and its ideal to de-activate the rod cell photoreceptor or rhodopsin over time.<ref name="variation">{{cite journal|last1=Sakurai|first1=Keisuke|last2=Young|first2=Joyce E.|last3=Kefalov|first3=Vladimir J.|last4=Khani|first4=Shahrokh C.|title=Variation in Rhodopsin Kinase Expression Alters the Dim Flash Response Shut Off and the Light Adaptation in Rod Photoreceptors|journal=Investigative Ophthalmology & Visual Science|date=29 August 2011|volume=52|issue=9|pages=6793|doi=10.1167/iovs.11-7158|accessdate=7 November 2016}}</ref> [[GRK1]] AND [[GRK7]]{{disambiguation needed|date=October 2017}}<!--Circular link?--> exist and are isoforms of rhodopsin kinase. Studies have proven that in mice rod cells, GRK1 has competition with [[arrestin]] for the binding site of [[rhodopsin]].<ref name="Sakurai">{{cite journal|last1=Sakurai|first1=Keisuke|last2=Chen|first2=Jeannie|last3=Khani|first3=Shahrokh C.|last4=Kefalov|first4=Vladimir J.|title=Regulation of Mammalian Cone Phototransduction by Recoverin and Rhodopsin Kinase|journal=Journal of Biological Chemistry|date=3 April 2015|volume=290|issue=14|pages=9239–9250|doi=10.1074/jbc.M115.639591|accessdate=7 November 2016|pmid=25673692|pmc=4423708}}</ref> Arrestin-1 when bound to rhodopsin inhibits signaling and turns off photo-transduction completely.<ref name="lodish">{{cite book|last1=Lodish|first1=Harvey|title=Molecular cell biology|date=2013|publisher=Worth Publ.|location=New York|isbn=978-1429234139|edition=Seventh edition.|accessdate=7 November 2016}}</ref> As is true for many enzymes, rhodopsin kinase is regulated by the activity of other proteins. In this case, it is negatively regulated by [[recoverin]] <ref>{{cite journal | title = Ca(2+)-Dependent Interaction of Recoverin with Rhodopsin Kinase in the Regulation of Rhodopsin Signaling |author1 = Chen, C.-K. |author2 = Inglese, J. |author3 = Lefkowitz, R.J.|author4 = Hurley, J.B.| journal = J. Biol. Chem.|date = 1995 |volume = 270 |pages = 18060–18065|pmid = 7629115 }}</ref>. In the dark state of the rod cells' [[recoverin]] inhibits rhodopsin kinase. Specifically, a study has proven that GRK1 acts on the cytoplasmic loops of rhodopsin both the second and third loops. The cytoplasmic loops act specifically where transducin binds to rhodopsin so this allows [[GRK1]] and [[transducin]] to compete for the binding site on rhodopsin. With [[recoverin]] present, it exists between [[GRK1]] and [[rhodopsin]] and it was shown that when bound competition between [[GRK1]] and [[transducin]] suppressed.<ref name="komolov">{{cite journal|last1=Komolov|first1=Konstantin E.|last2=Senin|first2=Ivan I.|last3=Kovaleva|first3=Nadezda A.|last4=Christoph|first4=Mathias P.|last5=Churumova|first5=Valeriya A.|last6=Grigoriev|first6=Ilya I.|last7=Akhtar|first7=Muhammad|last8=Philippov|first8=Pavel P.|last9=Koch|first9=Karl-Wilhelm|title=Mechanism of rhodopsin kinase regulation by recoverin|journal=Journal of Neurochemistry|date=July 2009|volume=110|issue=1|pages=72–79|doi=10.1111/j.1471-4159.2009.06118.x|accessdate=7 November 2016}}</ref>
Rhodopsin Kinase is involved in mammalian rod cells specifically with photo transduction and belongs to the family of G coupled-protein receptor kinases. This kinase, referred to as GRK1 is post-translationally modified by farnesylation and &alpha;-carboxyl methylation<ref>{{cite journal | vauthors = Inglese J, Glickman JF, Lorenz W, Caron MG, Lefkowitz RJ | title = Isoprenylation of a protein kinase. Requirement of farnesylation/alpha-carboxyl methylation for full enzymatic activity of rhodopsin kinase | journal = The Journal of Biological Chemistry | volume = 267 | issue = 3 | pages = 1422–5 | date = January 1992 | pmid = 1730692 }}</ref><ref name="kutuzov">{{cite journal | vauthors = Kutuzov MA, Andreeva AV, Bennett N | title = Regulation of the methylation status of G protein-coupled receptor kinase 1 (rhodopsin kinase) | journal = Cellular Signalling | volume = 24 | issue = 12 | pages = 2259–67 | date = December 2012 | pmid = 22846544 | doi = 10.1016/j.cellsig.2012.07.020 }}</ref> GRK1 phosphorylates rhodopsin, resulting in partial photo-activation of rhodopsin, thus activating the dim flash response.<ref name="Sakurai">{{cite journal | vauthors = Sakurai K, Chen J, Khani SC, Kefalov VJ | title = Regulation of mammalian cone phototransduction by recoverin and rhodopsin kinase | journal = The Journal of Biological Chemistry | volume = 290 | issue = 14 | pages = 9239–50 | date = April 2015 | pmid = 25673692 | pmc = 4423708 | doi = 10.1074/jbc.M115.639591 }}</ref> Dim flash response is activated in dim light and its ideal to de-activate the rod cell photoreceptor or rhodopsin over time.<ref name="variation">{{cite journal | vauthors = Sakurai K, Young JE, Kefalov VJ, Khani SC | title = Variation in rhodopsin kinase expression alters the dim flash response shut off and the light adaptation in rod photoreceptors | journal = Investigative Ophthalmology & Visual Science | volume = 52 | issue = 9 | pages = 6793–800 | date = August 2011 | pmid = 21474765 | doi = 10.1167/iovs.11-7158 | pmc=3176010}}</ref> [[GRK1]] AND [[G protein-coupled receptor kinase 7|GRK7]]<!--Circular link?--> exist and are isoforms of rhodopsin kinase. Studies have proven that in mice rod cells, GRK1 has competition with [[arrestin]] for the binding site of [[rhodopsin]].<ref name="Sakurai"/> Arrestin-1 when bound to rhodopsin inhibits signaling and turns off photo-transduction completely.<ref name="lodish">{{cite book|last1=Lodish|first1=Harvey|name-list-format=vanc|title=Molecular cell biology|date=2013|publisher=Worth Publ.|location=New York|isbn=978-1429234139|edition=Seventh edition.}}</ref> As is true for many enzymes, rhodopsin kinase is regulated by the activity of other proteins. In this case, it is negatively regulated by [[recoverin]].<ref>{{cite journal | vauthors = Chen CK, Inglese J, Lefkowitz RJ, Hurley JB | title = Ca(2+)-dependent interaction of recoverin with rhodopsin kinase | journal = The Journal of Biological Chemistry | volume = 270 | issue = 30 | pages = 18060–6 | date = July 1995 | pmid = 7629115 | doi=10.1074/jbc.270.30.18060}}</ref> In the dark state of the rod cells' [[recoverin]] inhibits rhodopsin kinase. Specifically, a study has proven that GRK1 acts on the cytoplasmic loops of rhodopsin both the second and third loops. The cytoplasmic loops act specifically where transducin binds to rhodopsin so this allows [[GRK1]] and [[transducin]] to compete for the binding site on rhodopsin. With [[recoverin]] present, it exists between [[GRK1]] and [[rhodopsin]] and it was shown that when bound competition between [[GRK1]] and [[transducin]] suppressed.<ref name="komolov">{{cite journal | vauthors = Komolov KE, Senin II, Kovaleva NA, Christoph MP, Churumova VA, Grigoriev II, Akhtar M, Philippov PP, Koch KW | title = Mechanism of rhodopsin kinase regulation by recoverin | journal = Journal of Neurochemistry | volume = 110 | issue = 1 | pages = 72–9 | date = July 2009 | pmid = 19457073 | doi = 10.1111/j.1471-4159.2009.06118.x }}</ref>


==See also==
== See also ==
* [[Rhodopsin]]
* [[Rhodopsin]]
* [[Beta adrenergic receptor kinase]]
* [[Beta adrenergic receptor kinase]]
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{{reflist}}
{{reflist}}


==External links==
== External links ==
* {{MeshName|Rhodopsin+kinase}}
* {{MeshName|Rhodopsin+kinase}}


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[[Category:EC 2.7.11]]
[[Category:EC 2.7.11]]


{{biochemistry-stub}}
{{biochemistry-stub}}

Latest revision as of 11:27, 9 January 2019

G protein-coupled receptor kinase 1
Identifiers
SymbolGRK1
Alt. symbolsRHOK
Entrez6011
HUGO10013
OMIM180381
RefSeqNM_002929
UniProtQ15835
Other data
EC number2.7.11.14
LocusChr. 13 q34

Rhodopsin kinase (EC 2.7.11.14, cone opsin kinase, G-protein-coupled receptor kinase 1, GPCR kinase 1, GRK1, GRK7, opsin kinase, opsin kinase (phosphorylating), rhodopsin kinase (phosphorylating), RK, STK14) is a serine/threonine-specific protein kinase involved in phototransduction.[1][2][3][4][5][6][7][8][9] This enzyme catalyses the following chemical reaction

ATP + rhodopsin <math>\rightleftharpoons</math> ADP + phosphorhodopsin

Mutations in rhodopsin kinase are associated with a form of night blindness called Oguchi disease.[10]

More on Rhodopsin Kinase

Rhodopsin Kinase is involved in mammalian rod cells specifically with photo transduction and belongs to the family of G coupled-protein receptor kinases. This kinase, referred to as GRK1 is post-translationally modified by farnesylation and α-carboxyl methylation[11][12] GRK1 phosphorylates rhodopsin, resulting in partial photo-activation of rhodopsin, thus activating the dim flash response.[13] Dim flash response is activated in dim light and its ideal to de-activate the rod cell photoreceptor or rhodopsin over time.[14] GRK1 AND GRK7 exist and are isoforms of rhodopsin kinase. Studies have proven that in mice rod cells, GRK1 has competition with arrestin for the binding site of rhodopsin.[13] Arrestin-1 when bound to rhodopsin inhibits signaling and turns off photo-transduction completely.[15] As is true for many enzymes, rhodopsin kinase is regulated by the activity of other proteins. In this case, it is negatively regulated by recoverin.[16] In the dark state of the rod cells' recoverin inhibits rhodopsin kinase. Specifically, a study has proven that GRK1 acts on the cytoplasmic loops of rhodopsin both the second and third loops. The cytoplasmic loops act specifically where transducin binds to rhodopsin so this allows GRK1 and transducin to compete for the binding site on rhodopsin. With recoverin present, it exists between GRK1 and rhodopsin and it was shown that when bound competition between GRK1 and transducin suppressed.[17]

See also

References

  1. ↑ Lorenz W, Inglese J, Palczewski K, Onorato JJ, Caron MG, Lefkowitz RJ (October 1991). "The receptor kinase family: primary structure of rhodopsin kinase reveals similarities to the beta-adrenergic receptor kinase". Proceedings of the National Academy of Sciences of the United States of America. 88 (19): 8715–9. doi:10.1073/pnas.88.19.8715. PMC 52580. PMID 1656454.
  2. ↑ Benovic JL, Mayor F, Somers RL, Caron MG, Lefkowitz RJ (1986). "Light-dependent phosphorylation of rhodopsin by beta-adrenergic receptor kinase". Nature. 321 (6073): 869–72. doi:10.1038/321869a0. PMID 3014340.
  3. ↑ Shichi H, Somers RL (October 1978). "Light-dependent phosphorylation of rhodopsin. Purification and properties of rhodopsin kinase". The Journal of Biological Chemistry. 253 (19): 7040–6. PMID 690139.
  4. ↑ Palczewski K, McDowell JH, Hargrave PA (October 1988). "Purification and characterization of rhodopsin kinase". The Journal of Biological Chemistry. 263 (28): 14067–73. PMID 2844754.
  5. ↑ Weller M, Virmaux N, Mandel P (January 1975). "Light-stimulated phosphorylation of rhodopsin in the retina: the presence of a protein kinase that is specific for photobleached rhodopsin". Proceedings of the National Academy of Sciences of the United States of America. 72 (1): 381–5. doi:10.1073/pnas.72.1.381. PMC 432309. PMID 164024.
  6. ↑ Cha K, Bruel C, Inglese J, Khorana HG (September 1997). "Rhodopsin kinase: expression in baculovirus-infected insect cells, and characterization of post-translational modifications". Proceedings of the National Academy of Sciences of the United States of America. 94 (20): 10577–82. doi:10.1073/pnas.94.20.10577. PMC 23407. PMID 9380677.
  7. ↑ Khani SC, Abitbol M, Yamamoto S, Maravic-Magovcevic I, Dryja TP (August 1996). "Characterization and chromosomal localization of the gene for human rhodopsin kinase". Genomics. 35 (3): 571–6. doi:10.1006/geno.1996.0399. PMID 8812493.
  8. ↑ Chen CK, Zhang K, Church-Kopish J, Huang W, Zhang H, Chen YJ, Frederick JM, Baehr W (December 2001). "Characterization of human GRK7 as a potential cone opsin kinase". Molecular Vision. 7: 305–13. PMID 11754336.
  9. ↑ Willets JM, Challiss RA, Nahorski SR (December 2003). "Non-visual GRKs: are we seeing the whole picture?". Trends in Pharmacological Sciences. 24 (12): 626–33. doi:10.1016/j.tips.2003.10.003. PMID 14654303.
  10. ↑ Yamamoto S, Sippel KC, Berson EL, Dryja TP (February 1997). "Defects in the rhodopsin kinase gene in the Oguchi form of stationary night blindness". Nature Genetics. 15 (2): 175–8. doi:10.1038/ng0297-175. PMID 9020843.
  11. ↑ Inglese J, Glickman JF, Lorenz W, Caron MG, Lefkowitz RJ (January 1992). "Isoprenylation of a protein kinase. Requirement of farnesylation/alpha-carboxyl methylation for full enzymatic activity of rhodopsin kinase". The Journal of Biological Chemistry. 267 (3): 1422–5. PMID 1730692.
  12. ↑ Kutuzov MA, Andreeva AV, Bennett N (December 2012). "Regulation of the methylation status of G protein-coupled receptor kinase 1 (rhodopsin kinase)". Cellular Signalling. 24 (12): 2259–67. doi:10.1016/j.cellsig.2012.07.020. PMID 22846544.
  13. ↑ 13.0 13.1 Sakurai K, Chen J, Khani SC, Kefalov VJ (April 2015). "Regulation of mammalian cone phototransduction by recoverin and rhodopsin kinase". The Journal of Biological Chemistry. 290 (14): 9239–50. doi:10.1074/jbc.M115.639591. PMC 4423708. PMID 25673692.
  14. ↑ Sakurai K, Young JE, Kefalov VJ, Khani SC (August 2011). "Variation in rhodopsin kinase expression alters the dim flash response shut off and the light adaptation in rod photoreceptors". Investigative Ophthalmology & Visual Science. 52 (9): 6793–800. doi:10.1167/iovs.11-7158. PMC 3176010. PMID 21474765.
  15. ↑ Lodish H (2013). Molecular cell biology (Seventh edition. ed.). New York: Worth Publ. ISBN 978-1429234139.
  16. ↑ Chen CK, Inglese J, Lefkowitz RJ, Hurley JB (July 1995). "Ca(2+)-dependent interaction of recoverin with rhodopsin kinase". The Journal of Biological Chemistry. 270 (30): 18060–6. doi:10.1074/jbc.270.30.18060. PMID 7629115.
  17. ↑ Komolov KE, Senin II, Kovaleva NA, Christoph MP, Churumova VA, Grigoriev II, Akhtar M, Philippov PP, Koch KW (July 2009). "Mechanism of rhodopsin kinase regulation by recoverin". Journal of Neurochemistry. 110 (1): 72–9. doi:10.1111/j.1471-4159.2009.06118.x. PMID 19457073.

External links

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