Retina International's Scientific Newsletter

	Retina International's Scientific Newsletter
Editor's Notes from literature on Rhodopsin Kinase (RHOK)

Recent update from: 19.12.1999

RHOK, GRK1

Notes

Isoprenylation depends on Cys 558

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (6)

RHOK

Notes

RHO-phosphorylation at bright light
Adaptation mechanism
Phosphorylates RHO at the loops between membran domains

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (11)

RHOK

Notes

Autophosphorylation

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (4)

RHOK

Notes

Binds recoverin
Phosphorylates RHO Ca²⁺ independent

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (2)

RHOK, GRK1

Notes

Phosphorylates RHO and bAR
Conserved site of autophosphorylation at Ser488 and Thr489
Cytosolic
Farnesylation is necessary for light-dependent translocation and full activation

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (5)

RHOK

Notes

RHOK is farnesylated and carboxymethylated

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (16)

RHOK

Notes

Phosphorylates only RHO C-terminal residues beyond Gly329
V-VI-loop is essential for kinase binding
Catalytic and interactive domain are different
Interacts only with the photolyzed form of RHO
Autophosphorylation is neccessary for membrane dissociation of RHOK

Species: Bos taurus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (13)

RHOK

Notes

Species: Bos taurus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers: Bovine

Protein Data

Aminoacids: 561 AA

Molecularweight	on SDS-PAGE: 62,9 kDa
	calculated:

Reference: (10)

RHOK

Notes

Not stimulated by cAMP, cGMP, or Ca²⁺
Does not phosphorylate histone
Soluble protein
In retina and pineal gland
N-terminus interacts with RHO
Farnesylation is necessary for full activity
Phosphorylation is not necessary for activity
Completely phosphorylated RHOK has lower RHO affinity
RHO phosphorylation is blocked by GNAT/GNB/G and partially inhibited by GNAT or GNB/G alone

Species: Bos taurus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids: 540 AA

Molecularweight	on SDS-PAGE: 63 kDa
	calculated:

Reference: (3)

RHOK

Notes

Isoprenylated
Isoprenyl groups are a mixture of C15 - C20
Glycosylation is deficient in baculovirus systems
Autophosphorylated at Ser-448, Ser-449 and rarely at Ser-21
C-terminal CVLS for farnesylation
Baculovirus system does not complete prenylation

Species: Bos taurus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (1)

RHOK

Notes

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons: 7

Primers: complete

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (17)

RHOK

Notes

Farnesylated posttranslationally at Cys 558
Serine/Threonine kinase
N-terminus plays role in RHO-binding
Autophosphorylates at Thr489 and Ser488 in bovine RHOK

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (9)

RHOK

Notes

Farnesylated posttranslationally at Cys 558
Serine/Threonine kinase
N-terminus plays role in RHO-binding
Autophosphorylates at Thr489 and Ser488 in bovine RHOK

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (9)

RHOK

Notes

84% cDNA, 92% protein homology to bovine

Species: Homo sapiens

See also:

Chromosomal localisation	in man: 13q34
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (7)

RHOK

Notes

Only in retina and pineal gland
Rod: loosely associated with membrane or cytosolic
No evidence for presence in cone cells
Utilizes freshly bleached Rho (MetaII)
Binds cytoplasmic loops
Needs Mg²⁺ > Mn²⁺
C-terminus not critical b
Not regulated by second messenger
Rod-specific Ca²⁺-binding protein may play regulating role
Subtrate: activated RHO
Activated by binding to cytoplasmic RHO loops
Autophosphorylation changes affinity

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE: 63 kDa
	calculated:

Reference: (12)

RHOK, GRK1

Notes

Ser/Thr kinase
Expression confined to the retina
Autophosphorylation sites at Ser21, Ser491, Thr492
Autoregulation by autophosphrylation
92% aminoacid and 84% nucleotide sequence identity to bovine
Likely to be isoprenylated
Interaction with RHO at residues 17 - 34
Myristoylation consensus sequence

Species: Homo sapiens

See also:

Chromosomal localisation	in man: 13q34
	in mouse:

Gene Data

Exons: 7

Primers:

Protein Data

Aminoacids: 564 AA

Molecularweight	on SDS-PAGE: 63,5 kDa
	calculated:

Reference: (8)

RHOK, GRK1, GRK1

Notes

Found almost exclusively in rods and cones
Ser/Thr protein kinase
Terminates signalling by the receptor
Requires post-translationally farnesylation

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE: 63 kDa
	calculated:

Reference: (14)

RHOK, GRK1, GRK1

Notes

requires post-translational farnesyl modification to bind light-activated RHO
Autophosphorylation at Ser484 and Thr485
High overall similarity to RHOK
abundant in lung, heart, retina, and linual epithelium
Light-dependent RHO phosphorylation
Phosphorylates C-terminus
No prenylation signal
Cloned from heart
Highest expression in heart, lung, retina

Species: Bos taurus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

mRNA: 2.8 kb + 7 kb

Exons:

Primers:

Protein Data

Aminoacids: 590 AA

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (15)

References:

1. Cha, K., Bruel, C., Inglese, J., and Khorana, H.G. Rhodopsin kinase: expression in baculovirus-infected insect cells, and characterization of post-translational modifications. 1997; Proc.Natl.Acad.Sci.U.S.A. 94: 10577 - 10582.
Goto Top Link to PudMed

2. Chen, C.K. and Hurley, J.B. Calcium dependent recoverin/rhodopsin kinase interaction. 1994; Invest.Ophthalmol.Vis.Sci. 35: 1485
Goto Top

3. Haga, T., Haga, K., and Kameyama, K. G protein--coupled receptor kinases. 1994; Journal.of.Neurochemistry. 63: 400 - 412.
Goto Top

4. Hargrave, P.A. and McDowell, J.H. Rhodopsin and phototransduction: a model system for G protein-linked receptors. 1992; FASEB Journal. 6: 2323 - 2331.
Goto Top Link to PudMed

5. Inglese, J., Freedman, N.J., Koch, W.J., and Lefkowitz, R.J. Structure and mechanism of the G protein-coupled receptor kinases. 1993; J.Biol.Chem. 268: 23735 - 23738.
Goto Top Link to PudMed

6. Inglese, J., Glickman, J.F., Lorenz, W., Caron, M.G., and Lefkowitz, R.J. Isoprenylation of a protein kinase. Requirement of farnesylation/alpha-carboxyl methylation for full enzymatic activity of rhodopsin kinase. 1992; J.Biol.Chem. 267: 1422 - 1425.
Goto Top Link to PudMed

7. Khani, S.C., Abitbol, M., Polans, A.S., Zhou, J., Asson-Batres, M.A., Palczewski, K., and Dryja, T.P. The nucleotide sequence of human rhodopsin kinase cDNA and the chromosomal localization of the gene. 1994; Invest.Ophthalmol.Vis.Sci. 35 (Suppl.): 1718
Goto Top

8. Khani, S.C., Abitbol, M., Yamamoto, S., Maravic Magovcevic, I., and Dryja, T.P. Characterization and chromosomal localization of the gene for human rhodopsin kinase. 1996; Genomics. 35: 571 - 576.
Goto Top Link to PudMed

9. Khani, S.C., Nielsen, L., and Vogt, T.M. Biochemical evidence for pathogenicity of rhodopsin kinase mutations correlated with the oguchi form of congenital stationary night blindness. 1998; Proc.Natl.Acad.Sci.U.S.A. 95: 2824 - 2827.
Goto Top Link to PudMed

10. Lorenz, W., Inglese, J., Palczewski, K., Onorato, J.J., Caron, M.G., and Lefkowitz, R.J. The receptor kinase family: primary structure of rhodopsin kinase reveals similarities to the beta-adrenergic receptor kinase. 1991; Proc.Natl.Acad.Sci.U.S.A. 88: 8715 - 8719.
Goto Top

11. Newton, A. and Williams, D.S. Protein kinase C in rod outer segments. 1992; Invest.Ophthalmol.Vis.Sci. 33 (Suppl.): 874
Goto Top

12. Palczewski, K. and Benovic, J.L. G-protein-coupled receptor kinases. 1991; Trends.Biochem.Sci. 16: 387 - 391.
Goto Top

13. Palczewski, K., Buczylko, J., Kaplan, M.W., Polans, A.S., and Crabb, J.W. Mechanism of rhodopsin kinase activation. 1991; J.Biol.Chem. 266: 12949 - 12955.
Goto Top

14. Premont, R.T., Inglese, J., and Lefkowitz, R.J. Protein kinases that phosphorylate activated G protein-coupled receptors. 1995; FASEB Journal. 9: 175 - 182.
Goto Top

15. Premont, R.T., Koch, W.J., Inglese, J., and Lefkowitz, R.J. Identification, purification, and characterization of GRK5, a member of the family of G protein-coupled receptor kinases. 1994; J.Biol.Chem. 269: 6832 - 6841.
Goto Top

16. Schafer, W.R. and Rine, J. Protein prenylation: genes, enzymes, targets, and functions. 1992; Annu.Rev.Genet. 26: 209 - 237.
Goto Top

17. 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. 1997; Nat.Gen. 15: 175 - 178.
Goto Top Link to PudMed

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Contact the editor: irpamp@irpa.org	This site is maintained and edited by Dr. rer. medic. Markus Preising, Dipl.Biol. Molecular Genetics Laboratory Department of Paediatric Ophthalmology, Strabismology and Ophthalmogenetics University of Regensburg Head: Prof. Dr. med. Birgit Lorenz