Retina International‘s Scientific Newsletter

Rhodopsin

Recent update from: 24.04.2005

RHO,

Notes

C110A/C187A resemble wild type in ground state folds correctly, binds 11 cis RAl
MII decays more than 20 times faster than wild type
C110S/C187S prevent chromophore formation
A/V replacement forms identical structure to Rho

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (9)

RHO,

Notes

Involved in ARRP

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (35)

RHO,

Notes

216 bp upstream enhancer in mouse and bovine

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (31)

RHO,

Notes

light changes COOH-terminus conformation to be more accessible in Metarhodopsin II
phosphorylated by Rhodopsin kinase at Ser and Thr at COOH-terminus
Palmitate attached to Cys 321/322
Co-translationally acetylated at NH-terminus
Glycosylated at Asn 2 and Asn 15

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (17)

RHO,

Notes

Phosphorylated only at C-Terminus

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (30)

RHO,

Notes

Mutation Thr58Arg: no spectral changes, reduced binding of transducin
Arg135: no spectral change, no transducin binding
del 68 - 71: no chromophor binding

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (27)

RHO,

Notes

5*10⁷ molecules / rod outer segment

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (40)

RHO,

Notes

Bovine Glu 134 Q/D => enhanced Gt activation mediates light dependend proton uptake by MII
MII = at RAl with unprotonated Schiff base
134D = Glu134 but slower proton uptake
134Q lack of proton uptake at pH6 small net release at pH7 normal at pH8

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (3)

RHO,

Notes

Ser338, Ser343 = 1. and 2. phosphorylation site
Ser 336 3. major phosphorylation site
SAG binding prevents further phosphorylation
Reduction of the photolysed chromophore prevents phosphorylation of more than 3 sites
Monophosphorylated at 343 or 338

Species:

See also: SAG

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (32)

RHO,

Notes

K296E causes no degeneration by continuously activating phototransduction
K286E is shut off by phototransduction inactivation mechanism
Mutant opsin is phosphorylated and stably bound by SAG
Light dependent

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (25)

RHO,

Notes

P9-10 acylation and glycosylation
No aberrant glycosylation in rd mice

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (37)

RHO,

Notes

Gly 90, Ala 292, Lys 196 mutations constitutively activated for phosphorylation by RK and activate GNAT
Binds tightly to SAG

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (15)

RHO,

Notes

Structural rearrangements: protonation of Glu113, cytoplasmic acidic residues => formation of meta II
Equilibrium between partially active (protonated) and inactive (deprotonated) RHO
Protonation of one or more carboxyl group is essential
Transition from meta I to meta II is accompanied by deprotonation of the Schiff-base
GNAt activation is pH dependent at pH 5-6

Species:

See also: GNT

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (6)

RHO,

Notes

Non-glycosylated Rho folds correctly
Strikingly light dependend Gt activation
Asn 2, Gly 3 or Thr 4 had no significant effect on folding, cellular transport or function
Asn 15 or Thr 17 activated GNAT poorly
Glycosylated by Man3GlcNAc3

Species:

See also: GNAT

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (24)

RHO,

Notes

Isomerization of 11cRAl reorganizes the contact surface of helices C and F

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (13)

RHO,

Notes

Artificial mutations of Arg 135 of RHO to Lys, Glu, Leu, Ala
Ala, Leu, Glu showed reduced GNAT activation
Ala was weakly phosphorylated
Ala and Leu weakly bind SAG in absence of 11cRAl

Species: Artificial

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (42)

RHO,

Notes

Acylation of RHO does not exhibit aging effect

Species: Bos taurus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (2)

RHO,

Notes

4 mutants of Arg 135 (Lys, Gln, Ala, Leu )
All of these mutants can bind and activate GNAT, are phosphorylated and bind SAG with 11cRal
They can be phosphorylated and bind SAG without bound 11cRal but do not activate GNAT
SAG binding was elevated particularly for R135A
GNAT activation was reduced 30 - 45 % for R135 Q,A,L
Arg 135 is critical for preventing phosphorylation and SAG binding
SAG binds even to unphosphorylated mutations

Species: Bos taurus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (36)

RHO,

Notes

Species: Bos taurus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (22)

RHO,

Notes

Steps Photo-Batho-BSI-Lumi-rhodopsin involve retinal portion
Steps Lumi-Meta I-Meta II-rhodopsin involve protein conformation
Binding of atRal to opsin creates pseudo-photoproducts capable of interacting with SAG
atRal-opsin-complex is non-covalent
atRal recombines with opsin independent of light

Species: Bos taurus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (21)

RHO,

Notes

In plasmamembrane and disk membrane

Species: Bos taurus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (8)

RHO,

Notes

1000 GNAT can be activated by one activated RHO
Cys 322 and 323 are palmitoylated
GNAT binding is an active process
Ribosylation of CYS347 block GNAT-RHO coupling

Species: Bos taurus

See also: GNT

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (16)

RHO,

Notes

Species: Drosophila melanogaster

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

cDNA:

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (44)

RHO,

Notes

Test of 13 Rh1 mutations (G69D,S95F,W116 X,G119E,P184L,E194K,G195S,W209X,G299E,W313X)
Rh1 requires ninaA as chaperon
Great majority of rho adRP mutations produce misfolded rho
Heterozygotes express 50% of wild type
Degeneration of ROS by interference of WT and mutant rho (Drosophila)
Pathogenic mechanism independent of activation of visual cascade
Mutants accumulate in ER overproliferation
Null mutations are recessive and act by gene dosage

Species: Drosophila melanogaster

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (4)

RHO,

Notes

Involved in RP4

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers: Man

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (11)

RHO,

Notes

Chromophor: 11cRAl
93,4% identity to bovine
TATA and CAAT-box

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

cDNA:

Exons: 5

Primers:

Protein Data

Amino acids: 348 AA

Molecular weight	on SDS-PAGE:
	calculated: 40000

Reference: (28)

RHO,

Notes

Investigation on P23H and G188R causing ADRP, as well as D190A and Y191/192del as artificial mutants
Folded RHO is resistant to trypsin digestion, misfolded RHO is degraded into small fragments

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (26)

RHO,

Notes

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

cDNA: 5,8 kb

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (5)

RHO,

Notes

Mutations in the helices cause RHO misfolding
Defects in packing of the helices are relayed to the intradiscal domain

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (20)

RHO,

Notes

Species: Homo sapiens

See also:

Chromosomal localisation	in man: 3q21-q24
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (39)

RHO,

Notes

Leu 125 Phe showed abnormal bleaching behaviour, reduced transducin activation and destabilized metarhodopsin II

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (14)

RHO,

Notes

Glu 134 and Arg 135 mutations cause altered GDP release from GNAT
Constitute the site that provides signal from RHO to GNAT
Peripherally associated with GNAT in the GDP-bound state when non-activated
Glu 134 and Arg 135 mutations do not affect expression level nor glycosylation pattern
Mutants revealed maximum spectral sensitivity at 380 nm => formation of MII
E134Q-R135Q, R135G, and R135Q mutant did not activate GTP binding activity of GNAT

Species: Homo sapiens

See also: GNAT

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (1)

RHO,

Notes

Maximum absorption at 495 nm

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (29)

RHO,

Notes

P23H N-terminus is truncated and non-glycosylated
Gly 90 Asp: RHO density in vivo is normal

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (23)

RHO,

Notes

Promoter: Eopsin-Ret/PCE-BAT-1-NRE-Ret4-TATA
ca. 3.3 kb promoter size

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (43)

RHO,

Notes

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse: 3

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (38)

RHO,

Notes

Mouse model for retinopathy
Insertion into exon II
Heterozygotes had thinned outer nuclear layer
Homozygotes lost ERG response at 8 weeks of age

Species: Mus musculus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (19)

Rho,

Notes

Linked to Raf-1

Species: Mus musculus

See also:

Chromosomal localisation	in man:
	in mouse: 6 distal

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (12)

RHO,

Notes

Transgenic mice with deleted phosphorylation sites
S334X: rods failed to make outer segment
Cone ERG was normal
Reduced a-waves on reduced ISI
Dim flash strengths prolong only few rod responses, greater flash strengths prolong all
Rod mediated a-waves were slightly below normal on sufficient ISI

Species: Mus musculus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (7)

RHO,

Notes

Species: Octopus spec.

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

cDNA:

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (33)

RHO,

Notes

Dephosphorylation rate is increased by DOPA
ROS of DOPA-treated retinas contain increased RHO-phosphatase activity
RHO dephosphorylation appears to be affected by Ca²⁺ and a Ca²⁺-sensitive phosphatase
Phosphorylation rate after DOPA treatment is similar to control
After DOPA treatment RHO-P decreased up to 50% at 45 min, with RHO being dephosphorylated at a faster rate
DOPA-treated ROS cytosol contained more RHO-phosphatase activity

Species: Rana catesbeiana

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (41)

rho,

Notes

Observed first at PN5 coincident with ROS development

Species: Rattus norvegicus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (18)

RHO,

Notes

4 synthetic mutations at Gly 90D, Glu 113Q, Ala292E, Lys296G/E/M
Mutants constitutively activate RHO for activation of GNT even without light
In addition these mutants are constitutively phosphorylated by RHOK for inactivation
SAG binds to phosphorylated mutants
GNAT and RHOK recognize the same conformational change in RHO
After SAG binding RAl cannot reverse these reactions, therefore RHO-SAG complexes accumulate inside photoreceptors

Species: Synthetic

See also: GNT

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (34)

RHO,

Notes

rab 6 drives RHO through TGN
rab 8 takes RHO post Golgi to membrane
C-terminal conserved sequence QVS(A)PA: frog - QVSPA; vertebrates: QVAPA
Mutation result in missorting in the TGN

Species: synthetic

See also: RAB

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Amino acids:

Molecular weight	on SDS-PAGE:
	calculated:

Reference: (10)

References

Acharya,S. and Karnik,S.S. Modulation of GDP release from transducin by the conserved Glu134-Arg135 sequence in rhodopsin. 1996; J.Biol.Chem. 271: 25406-25411. Goto Top
Albert,A.D., Yeagle,P.L., Alderfer,J.L., Dorey,M., Vogt,T., Bhawsar,N., Hargrave,P.A., McDowell,J.H., and Arendt,A. Phosphorylation Alters The Three Dimensional Structure Of The Carboxyl Terminal Of Bovine Rhodopsin. 1997; Invest.Ophthalmol.Vis.Sci. 38: S593-A1000 Goto Top
Arnis,S., Fahmy,K., Hofmann,K.P., and Sakmar,T.P. A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin. 1994; J.Biol.Chem. 269: 23879-23881. Goto Top
Baker,E.K., Colley,N.J., and Zuker,C.S. The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin. 1994; EMBO J. 13: 4886-4895. Goto Top
Bennett,J. and Sun,D. DNA sequence of the 5.8 kb region upstream to the human rhodopsin gene. 1993; Invest.Ophthalmol.Vis.Sci. 34: 809 Goto Top
Buczylko,J., Saari,J.C., Crouch,R.K., and Palczewski,K. Mechanisms of opsin activation. 1996; J.Biol.Chem. 271: 20621-20630. Goto Top
Chen,C.K., Inglese,J., Lefkowitz,R.J., and Hurley,J.B. Ca(2+)-dependent interaction of recoverin with rhodopsin kinase. 1995; J.Biol.Chem. 270: 18060-18066. Goto Top
Cook,N.J., Molday,L.L., Reid,D., Kaupp,U.B., and Molday,R.S. The cGMP-gated channel of bovine rod photoreceptors is localized exclusively in the plasma membrane. 1989; J.Biol.Chem. 264: 6996-6999. Goto Top
Davidson,F.F., Loewen,P.C., and Khorana,H.G. Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state. 1994; Proc.Natl.Acad.Sci.U.S.A. 91: 4029-4033. Goto Top
Deretic,D. Post-Golgi trafficking of rhodopsin in retinal photoreceptors. 1998; Eye. 12: 526-530.
Goto Top
Dryja,T.P., Hahn,L.B., Cowley,G.S., McGee,T.L., and Berson,E.L. Mutation spectrum of the rhodopsin gene among patients with autosomal dominant retinitis pigmentosa. 1991; Proc.Natl.Acad.Sci.U.S.A. 88: 9370-9374.
Goto Top
Elliott,R.W., Sparkes,R.S., Mohandas,T., Grant,S.G., and McGinnis,J.F. Localization of the rhodopsin gene to the distal half of mouse chromosome 6. 1990; Genomics. 635-644. Goto Top
Farrens,D.L., Altenbach,C., Yang,K., Hubbell,W.L., and Khorana,H.G. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. 1996; Science. 274: 768-770. Goto Top
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. 1996; Proc.Natl.Acad.Sci.U.S.A. 93: 4560-4564. Goto Top
Gurevich,V.V., Dion,S.B., Onorato,J.J., Ptasienski,J., Kim,C.M., Sterne-Marr,R., Hosey,M.M., and Benovic,J.L. Arrestin interactions with G protein-coupled receptors. Direct binding studies of wild type and mutant arrestins with rhodopsin, beta 2-adrenergic, and m2 muscarinic cholinergic receptors. 1995; J.Biol.Chem. 270: 720-731. Goto Top
Hamm,H.E. Molecular interactions between the photoreceptor G protein and rhodopsin. 1991; Cell Mol.Neurobiol. 11: 563-578. Goto Top
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
He,L., Swaroop,A., and Fox,D.A. Spatiotemporal Pattern Of NRL In The Developing Rat Retina. 1998; Invest.Ophthalmol.Vis.Sci. 39: S197 Goto Top
Humphries,M.M., Rancourt,D., Farrar,G.J., Kenna,P., Hazel,M., Bush,R.A., Sieving,P.A., Sheils,D.M., McNally,N., Creighton,P., Erven,A., Boros,A., Gulya,K., Capecchi,M.R., and Humphries,P. Retinopathy induced in mice by targeted disruption of the rhodopsin gene. 1997; Nat.Genet. 15: 216-219.
Goto Top
Hwa,J., Garriga,P., Liu,X., and Khorana,H.G. Structure and function in rhodopsin: packing of the helices in the transmembrane domain and folding to a tertiary structure in the intradiscal domain are coupled. 1997; Proc.Natl.Acad.Sci.U.S.A. 94: 10571-10576.
Goto Top
Jager,S., Palczewski,K., and Hofmann,K.P. Opsin/all-trans-retinal complex activates transducin by different mechanisms than photolyzed rhodopsin. 1996; Biochemistry. 35: 2901-2908.
Goto Top
Jager,S., Szundi,I., Lewis,J.W., Mah,T.L., and Kliger,D.S. Effects of pH on rhodopsin photointermediates from lumirhodopsin to metarhodopsin II. 1998; Biochemistry. 37: 6998-7005.
Goto Top
Jin,J., Heth,C.A., and Roof,D.J. P23H mutant opsin in transgenic murine retina, truncation of N- terminus and lack of glycosylation. 1995; Invest.Ophthalmol.Vis.Sci. 36: S424 Goto Top
Kaushal,S., Ridge,K.D., and Khorana,H.G. Structure and function in rhodopsin: the role of asparagine- linked glycosylation. 1994; Proc.Natl.Acad.Sci.U.S.A. 91: 4024-4028.
Goto Top
Li,T., Franson,W.K., Gordon,J.W., Berson,E.L., and Dryja,T.P. Constitutive activation of phototransduction by K296E opsin is not a cause of photoreceptor degeneration. 1995; Proc.Natl.Acad.Sci.U.S.A. 92: 3551-3555.
Goto Top
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. 1996; Proc.Natl.Acad.Sci.U.S.A. 93: 4554-4559. Goto Top
Min,K.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. 1993; J.Biol.Chem. 268: 9400-9404. Goto Top
Nathans,J. and Hogness,D.S. Isolation and nucleotide sequence of the gene encoding human rhodopsin. 1984; Proc.Natl.Acad.Sci.U.S.A. 81: 4851-4855.
Goto Top
Nathans,J., Thomas,D., and Hogness,D.S. Molecular genetics of human color vision: the genes encoding blue, green, and red pigments. 1986; Science. 232: 193-202.
Goto Top
Newton,A.C. and Williams,D.S. Rhodopsin is the major in situ substrate of protein kinase C in rod outer segments of photoreceptors. 1993; J.Biol.Chem. 268: 18181-18186.
Goto Top
Nir,I., Zhao,Y., and Zack,D.J. Regulation of rhodopsin gene expression transgenic mouse studies of a distal regulatory element. 1993; Invest.Ophthalmol.Vis.Sci. 34: 809 Goto Top
Ohguro,H., Johnson,R.S., Ericsson,L.H., Walsh,K.A., and Palczewski,K. Control of rhodopsin multiple phosphorylation. 1994; Biochemistry. 33: 1023-1028.
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Contact the editor	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