Retina International's Scientific Newsletter

	Retina International's Scientific Newsletter
Editor's Notes from literature on Arrestin (SAG)

Recent update from: 18.12.1999

SAG,

Notes

SAG speeds up the process of RHO inactivation at 0.5 - 1.4 phosphate/RHO
SAG may only have a role at high level of bleaching
SAG binds to RHO at low phosphorylation levels

Species:

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (3)

SAG,

Notes

Activates PLCb1

Species: Bos taurus

See also: PLCb1

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (13)

SAG,

Notes

Species: Bos taurus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

cDNA:

Exons:

Primers:

Protein Data

Aminoacids: 404 AA

Molecularweight	on SDS-PAGE:
	calculated: 45275

Reference: (33)

SAG,

Notes

Ultrazentrifugation gives 42 - 44 kDa, SDS-PAGE estimates 50 kDa
RHO : SAG 1:1
Binds phosphorylated RHO

Species: Bos taurus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

cDNA:

Exons:

Primers:

Protein Data

Aminoacids: 239 AA

Molecularweight	on SDS-PAGE:
	calculated: 26822

Reference: (43)

SAG,

Notes

Species: Bos taurus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE: 48 kDa
	calculated:

Reference: (42)

SAG,

Notes

Binds and hydrolyzes ATP
Capacity: 2 mol ATP
Half saturation at 0.1 microM free ATP
ATP binding inhibits RHO binding prior to phosphorylation by RHOK
Contradiction: ATPase of ROS should be strongly membrane bound unlike SAG
ATP-binding sites are not involved in RHO binding
Possible effect: (a) SAG inhibits more RHO molecules than possible by the number of free SAG molecules; (b) SAG binding induces conformational change starting RHO regeneration

Species: Bos taurus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (14)

SAG,

Notes

AA 330-370 most prevalent binding region to RHO

Species: Bos taurus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (38)

Arr2,

Notes

deactivates MetaII in photoreceptor cells
responsible for light dependent photoreceptor degeneration in Drosophila

Species: Drosophila melanogaster

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids: 401 AA

Molecularweight	on SDS-PAGE: 48 kDa
	calculated:

Reference: (8)

SAG,

Notes

Identity 40% to human or bovine
TATAA-box at -27

Species: Drosophila melanogaster

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

cDNA:

Exons: 4

Primers:

Protein Data

Aminoacids: 346 AA

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (36)

Arr1,

Notes

Artifical mutations cause prolonged depolarization afterpotential
in the absence of Arr photoreceptors undergo light-dependent retinal degeneration
51% homology to Arr2, 48% homology to vertebrate SAG

Species: Drosophila melanogaster

See also: RHO

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids: 364 AA

Molecularweight	on SDS-PAGE: 37 kDa
	calculated:

Reference: (8)

SAG,

Notes

MetaRho is substrate for RHOK
Arr-Meta is a stable complex in the dark but can isomerize on photon uptake
Loss of Arr leads to prolonged depolarizing afterpotential
Phosphorylation and G protein dissociation do not significantly influence the rate of photoreceptor inactivation

Species: Drosophila melanogaster

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (29)

Arr,

Notes

Species: Drosophila miranda

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

cDNA:

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE: 49 kDa
	calculated:

Reference: (21)

SAG,

Notes

Inhibits RHOK

Species: Homo sapiens

See also: RHO

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (28)

SAG,

Notes

Species: Homo sapiens

See also:

Chromosomal localisation	in man: 2q34-q37
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE: 45 kDa
	calculated:

Reference: (26)

XAR,

Notes

transcription start site 21 bp upstream ATG
Promotor: TATA, CCAAT, Helix-Loop-Helix, PCE-1 like element
1 mutation in 30 cases: exon 12 Thr 299 Cys CCG -> CTG not confirmed

Species: Homo sapiens

See also:

Chromosomal localisation	in man: Xcen - q21
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (16)

XAR,

Notes

in inner and outer segments of retina

Species: Homo sapiens

See also:

Chromosomal localisation	in man: Xq
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids: 388 AA

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (32)

SAG,

Notes

Markers: D2S23, D2S55; D2S172, CRYGa

Species: Homo sapiens

See also:

Chromosomal localisation	in man: 2q34-37
	in mouse:

Gene Data

Exons:

Primers: Exon 16

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (41)

SAG,

Notes

single copy gene
No TATA-, GC-, CAAT-box
genomic DNA: 50 kb
Exon/Intron-boundaries
Single gene

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

mRNA: 1.9 kb

Exons: 16

Primers:

Protein Data

Aminoacids: 403 AA

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (45)

CAR,

Notes

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

gDNA: 20 kb

Exons: 17

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (16)

SAG,

Notes

Conserved photoreceptor promotor element PCE1

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (19)

SAG,

Notes

Negates involvement in RP
526 patients, ADRP, ARRP, RP simplex

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (30)

SAG,

Notes

Calcineurin is responsible for SAG dephosphorylation

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)

SAG,

Notes

binds ATP and Ca2+

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (15)

SAG,

Notes

Exon - intron bounderies
Differences to published sequences

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers: Exons 2 - 14

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (35)

SAG,

Notes

p44 truncated C-terminus in bovine rods
Strongly inhibits GNAT activation by dephosphorylated RHO
Splice variant at Ser369
Arrestin inhibits dephosphorylation of RHO
p44 binds activly to both RHO* and RHO*P

Species: Homo sapiens

See also: RHO

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (39)

SAG,

Notes

Binds MetaII und MetaII-P for regulation
Homology to bovine 81%
Local sequence similarities to G-protein

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

cDNA:

Exons:

Primers:

Protein Data

Aminoacids: 405 AA

Molecularweight	on SDS-PAGE:
	calculated: 45050

Reference: (46)

SAG,

Notes

In Drosophila immunoreactivity with ocelli

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (23)

SAG,

Notes

Comparable immunoreactivity in Bovine, Man, Mouse, Rat

Species: Homo sapiens

See also:

Chromosomal localisation	in man: 2q33-q34
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (34)

SAG,

Notes

Rat mRNA level increases on change light -> darkness

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (10)

SAG,

Notes

SAG localizes during light phase mostly in OS- during darkphase mostly in IS, nuclei and synaptic termini
Disc domains label at low density - cytoplasmic domains label at high density
No label of cytoplasmic regions in illuminated retina

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (27)

SAG,

Notes

Oguchi disease D2S172 - D2S345
homozygous 1147 del A, codon 309 Asn in Japanese

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers: Exons 2 -16

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (11)

SAG,

Notes

Species: Homo sapiens

See also:

Chromosomal localisation	in man: 2q37
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (4)

CAR,

Notes

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons: 13

Primers:

Protein Data

Aminoacids: 388 AA

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (32)

SAG,

Notes

Val 170 -> Arg 182 binds phosphorylated RHO-C-terminus

Species: Homo sapiens

See also: RHO

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (17)

SAG,

Notes

Binds Rho at 3rd cytoplasmic loop of Rho
3 domains: phosphorylation recognition site, activation recognition site, hydrophobic booster site
Strict selectivity of Sag for RHO-P*
Multisite interaction of SAG to loop 1 and 3 of RHO

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (22)

Arr,

Notes

Arr can be phosphorylated at three sites near the N-terminus
Interactions with RHO may depend on the extent

Species: Limulus spec.

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (2)

SAG,

Notes

Species: Limulus spec.

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids: 400 AA

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (37)

Sag,

Notes

Knock-out mice effective at -/- not effective at +/-
Effective in shut-off of response

Species: Mus musculus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (44)

SAG,

Notes

Species: Mus musculus

See also:

Chromosomal localisation	in man:
	in mouse: 1

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (6)

Sag,

Notes

SAG knockout
Very slow recovery of rod responses
Cells are alive
Cone responses are more or less normal

Species: Mus musculus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (24)

SAG,

Notes

Homology to bovine 84%

Species: Mus musculus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

cDNA: 1.6 - 1.7 kb

Exons:

Primers:

Protein Data

Aminoacids: 403 AA

Molecularweight	on SDS-PAGE:
	calculated: 44930

Reference: (40)

SAG,

Notes

rds retinae lack diurnal rythm of SAG mRNA expression
rds retinae maintain high levels of SAG expression at light and darkness
several members of the arrestin family are expressed in the retina

Species: Mus musculus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (1)

Sag,

Notes

Knock-out modell effective as -/-
At dim flashes normal ERG
Abnormality in final shut off
Sag is necessary for normal shutoff but not adaptation

Species: Mus musculus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (7)

SAG,

Notes

Species: Mus musculus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons: 16

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (34)

Sag,

Notes

Proximal promotor at posiion -38 - +304 is sufficient to direct low levels of retina-specific expression
Sequences up to -209 show higher expression levels and expression in lens, brain, and pineal gland
No TATA-, GC-, or CAAT-box
Direct repeat hexamer at position -205 - -185 is bound by factor Bd
Bp1(PCEI), Bp2, Bp3 bind to -25 - -15

Species: Mus musculus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (18)

XAR,

Notes

in inner and outer segments of retina
49% homology to human retinal arrestin
immunoreactivity in retina and IPL

Species: Xenopus laevis

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (25)

ARRB1, beta 1

Notes

ARRB1 is inhibitor of beta-Andrenergic receptor

Species: Homo sapiens

See also:

Chromosomal localisation	in man: 11q13
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (4)

ARRB2, beta 2

Notes

Species: Homo sapiens

See also:

Chromosomal localisation	in man: 17p13
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (4)

CAR, cone

Notes

IR in red-, green-, and blue -sensitive cones
Greatest IR in outer segments

Species: Homo sapiens

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE: 47 kDa
	calculated:

Reference: (31)

CAR, cone

Notes

IP=5.71

Species: Homo sapiens

See also:

Chromosomal localisation	in man: X
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids: 387 AA

Molecularweight	on SDS-PAGE:
	calculated: 42519

Reference: (5)

CAR, cone

Notes

Species: Homo sapiens

See also:

Chromosomal localisation	in man: Xp21-p11
	in mouse:

Gene Data

Exons: 16

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (12)

SAG, retinal

Notes

COUP factor binds TGACCNNNTGACC motif
SAG has hormonal response element (HRE) TGACCT(N7)TGACCT
COUP recognizes HRE in SAG

Species: Bos taurus

See also:

Chromosomal localisation	in man:
	in mouse:

Gene Data

Exons:

Primers:

Protein Data

Aminoacids:

Molecularweight	on SDS-PAGE:
	calculated:

Reference: (20)

References:

1. Agarwal, N., Nir, I., and Papermaster, D.S. Loss of diurnal arrestin gene expression in rds mutant mouse retinas. 1994; Exp.Eye Res. 58: 1 - 8.
Goto Top

2. Battelle, B.A., Reinke, E.D., Brink, C.M., Hargrave, P.A., and Smith, W.C. Multiple Phosphorylation Of Limulus Arrestin. 1996; Invest.Ophthalmol.Vis.Sci. S807
Goto Top

3. Bennett, N. and Sitaramayya, A. Inactivation of photoexcited rhodopsin in retinal rods: the roles of rhodopsin kinase and 48-kDa protein (arrestin). 1988; Biochemistry. 27: 1710 - 1715.
Goto Top

4. Calabrese, G., Sallese, M., Stornaiuolo, A., Stuppia, L., Palka, G., and Deblasi, A. Chromosome mapping of the human arrestin (SAG), beta- arrestin 2 (ARRB2), and beta-adrenergic receptor kinase 2 (ADRBK2) genes. 1994; Genomics. 23: 286 - 288.
Goto Top

5. Craft, C.M., Whitmore, D.H., and Wiechmann, A.F. Cone arrestin identified by targeting expression of a functional family. 1994; J.Biol.Chem. 269: 4613 - 4619.
Goto Top Link to PudMed

6. Danciger, M., Kozak, C.A., Tsuda, M., Shinohara, T., and Farber, D.B. The gene for retinal S-antigen (48-kDa protein) maps to the centromeric portion of mouse chromosome 1 near Idh-1. 1989; Genomics. 5: 378 - 381.
Goto Top

7. Dodd, R.L., Makino, C.L., Xu, J., Chen, J., Simon, M.I., and Baylor, D.A. Knockout of Arrestin Delays Final shutoff of the Rod Photoresponse. 1996; Invest.Ophthalmol.Vis.Sci. 37: S5
Goto Top

8. Dolph, P.J., Ranganathan, R., Colley, N.J., Hardy, R.W., Socolich, M., and Zuker, C.S. Arrestin function in inactivation of G protein-coupled receptor rhodopsin in vivo. 1993; Science. 260: 1910 - 1916.
Goto Top

9. Edwards, S.C., Ellis, D.Z., and Herrera, D.C. Evidence that calcineurin is responsible for arrestin dephosphorylation in the limulus lateral eye. 1993; Invest.Ophthalmol.Vis.Sci. 34 (Suppl.): 1325
Goto Top

10. Farber, D.B., Danciger, J.S., and Organisciak, D.T. Levels of mRNA encoding proteins of the cGMP cascade as a function of light environment. 1991; Exp.Eye Res. 53: 781 - 786.
Goto Top

11. 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. 1995; Nat.Genet. 10: 360 - 362.
Goto Top Link to PudMed

12. Gerber, S., Rozet, J.M., Vandepol, T.J.R., Hoyng, C.B., Munnich, A., Blankenagel, A., Kaplan, J., and Cremers, F.P.M. Complete Exon-Intron Structure Of The Retina-Specific ATP Binding Transporter Gene (ABCR) Allows The Identification Of Novel Mutations Underlying Stargardt-Disease. 1998; Genomics. 48: 139 - 142.
Goto Top

13. Ghalayini, A.J. and Anderson, R.E. Activation of bovine rod outer segment phospholipase C by arrestin. 1992; J.Biol.Chem. 267: 17977 - 17982.
Goto Top

14. Glitscher, W. and Ruppel, H. Evidence for ATP-ase activity of arrestin from bovine photoreceptors. 1991; FEBS Letters. 282: 431 - 435.
Goto Top

15. 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

16. Inana, G., Sakuma, H., Higashide, T., Yajima, T., McLaren, M.J., and Murakami, A. Cloning, characterization, and candidate gene analysis of the gene encoding X-arrestin, a new retinal arrestin. 1995; Invest.Ophthalmol.Vis.Sci. 36: S222
Goto Top

17. Kieselbach, T., Irrgang, K.D., and Ruppel, H. A segment corresponding to amino acids Val170-Arg182 of bovine arrestin is capable of binding to phosphorylated rhodopsin. 1994; Eur.J.Biochem. 226: 87 - 97.
Goto Top

18. Kikuchi, T., Raju, K., Breitman, M.L., and Shinohara, T. The proximal promoter of the mouse arrestin gene directs gene expression in photoreceptor cells and contains an evolutionarily conserved retinal factor-binding site. 1993; Mol.Cell Biol. 13: 4400 - 4408.
Goto Top Link to PudMed

19. Kikuchi, T. and Shinohara, T. Photoreceptor conserved element (PCE-1) associated with photoreceptor specific. promotor activity were found in arrestin genes of -12 to -24 of the mouse and first intron of bovine. 1994; Invest.Ophthalmol.Vis.Sci. 35: 1578
Goto Top

20. Kimura, H., Ogura, Y., Miyamoto, H., Yasukawa, T., Honda, Y., Tabata, Y., and Ikada, Y. Cationic Gelatin As A Gene Transfer Vector. 1997; Invest.Ophthalmol.Vis.Sci. 38: S1132 - A1000.
Goto Top

21. Krishnan, R. and Ganguly, R. Nucleotide sequence of the arrestin-like 49 Kd protein gene of Drosophila miranda. 1990; Nucleic.Acids.Res. 18: 5894
Goto Top

22. Krupnick, J.G., Gurevich, V.V., Schepers, T., Hamm, H.E., and Benovic, J.L. Arrestin-rhodopsin interaction. Multi-site binding delineated by peptide inhibition. 1994; J.Biol.Chem. 269: 3226 - 3232.
Goto Top

23. Lieb, W.E., Smith Lang, L., Dua, H.S., Christensen, A.C., and Donoso, L.A. Identification of an S-antigen-like molecule in Drosophila melanogaster: an immunohistochemical study. 1991; Exp.Eye Res. 53: 171 - 178.
Goto Top

24. Lyubarsky, A.L., Pugh, E.N., Falsini, B., Valentini, P., and Chen, J. Arrestin Knock-Out Mice As A Model Of Oguchi's Disease. 1998; Invest.Ophthalmol.Vis.Sci. 39: S643
Goto Top

25. Murakami, A., Yajima, T., Sakuma, H., McLaren, M.J., and Inana, G. X-arrestin: a new retinal arrestin mapping to the X chromosome. 1993; FEBS Letters. 334: 203 - 209.
Goto Top

26. Ngo, J.T., Klisak, I., Sparkes, R.S., Mohandas, T., Yamaki, K., Shinohara, T., and Bateman, J.B. Assignment of the S-antigen gene (SAG) to human chromosome 2q24-q37. 1990; Genomics. 7: 84 - 87.
Goto Top Link to PudMed

27. Nir, I. and Ransom, N. Ultrastructural analysis of arrestin distribution in mouse photoreceptors during dark/light cycle. 1993; Exp.Eye Res. 57: 307 - 318.
Goto Top

28. Palczewski, K., McDowell, J.H., Jakes, S., Ingebritsen, T.S., and Hargrave, P.A. Regulation of rhodopsin dephosphorylation by arrestin. 1989; J.Biol.Chem. 264: 15770 - 15773.
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29. Ranganathan, R., Malicki, D.M., and Zuker, C.S. Signal transduction in Drosophila photoreceptors. 1995; Annual.Review.of.Neuroscience. 18: 283 - 317.
Goto Top

30. Ringens, P.J., Fang, M., Shinohara, T., Bridges, C.D., Lerea, C.L., Berson, E.L., and Dryja, T.P. Analysis of genes coding for S-antigen, interstitial retinol binding protein, and the alpha-subunit of cone transducin in patients with retinitis pigmentosa. 1990; Invest.Ophthalmol.Vis.Sci. 31: 1421 - 1426.
Goto Top Link to PudMed

31. Sakuma, H., Inana, G., Murakami, A., Higashide, T., and McLaren, M.J. Immunolocalization of X-arrestin in human cone photoreceptors. 1996; FEBS Letters. 382: 105 - 110.
Goto Top

32. Sakuma, H., Murakami, A., Yajima, T., McLaren, M.J., and Inana, G. Cloning and analysis of X-arrestin: A new retinal arrestin mapping to the X chromosome. 1994; Invest.Ophthalmol.Vis.Sci. 35: 1265
Goto Top

33. Shinohara, T., Dietzschold, B., Craft, C.M., Wistow, G., Early, J.J., Donoso, L.A., Horwitz, J., and Tao, R. Primary and secondary structure of bovine retinal S antigen (48-kDa protein). 1987; Proc.Natl.Acad.Sci.U.S.A. 84: 6975 - 6979.
Goto Top

34. Shinohara, T., Singh, V.K., Tsuda, M., Yamaki, K., Abe, T., and Suzuki, S. S-antigen: from gene to autoimmune uveitis. 1990; Exp.Eye Res. 50: 751 - 757.
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35. Sippel, K.C., DeStefano, J.D., Berson, E.L., and Dryja, T.P. Evaluation of the human arrestin gene in patients with retinitis pigmentosa and stationary night blindness. 1998; Invest.Ophthalmol.Vis.Sci. 39: 665 - 670.
Goto Top Link to PudMed

36. Smith, D.P., Shieh, B.H., and Zuker, C.S. Isolation and structure of an arrestin gene from Drosophila. 1990; Proc.Natl.Acad.Sci.U.S.A. 87: 1003 - 1007.
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37. Smith, K.H., Johns, D.R., Heher, K.L., and Miller, N.R. Heteroplasmy in Leber's hereditary optic neuropathy. 1993; Arch.Ophthalmol. 111: 1486 - 1490.
Goto Top Link to PudMed

38. Smith, W.C. and Hargrave, P.A. Mapping Portions Of Arrestin That Bind To Rhodopsin Using Phage Display. 1997; Invest.Ophthalmol.Vis.Sci. 38: S23 - A1000.
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39. Smith, W.C., Milam, A.H., Dugger, D., Arendt, A., Hargrave, P.A., and Palczewski, K. A splice variant of arrestin. Molecular cloning and localization in bovine retina. 1994; J.Biol.Chem. 269: 15407 - 15410.
Goto Top Link to PudMed

40. Tsuda, M., Syed, M., Bugra, K., Whelan, J.P., McGinnis, J.F., and Shinohara, T. Structural analysis of mouse S-antigen. 1988; Gene. 73: 11 - 20.
Goto Top

41. Valverde, D., Bayes, M., Martinez, I., Grinberg, D., Vilageliu, L., Balcells, S., Gonzalez Duarte, R., and Baiget, M. Genetic fine localization of the arrestin (S-antigen) gene 4 cM distal from D2S172. 1994; Hum.Genet. 94: 193 - 194.
Goto Top

42. Wilden, U., Wust, E., Weyand, I., and Kuhn, H. Rapid affinity purification of retinal arrestin (48 kDa protein) via its light-dependent binding to phosphorylated rhodopsin. 1986; FEBS Letters. 207: 292 - 295.
Goto Top

43. Wistow, G.J., Katial, A., Craft, C., and Shinohara, T. Sequence analysis of bovine retinal S-antigen. Relationships with alpha-transducin and G-proteins. 1986; FEBS Letters. 196: 23 - 28.
Goto Top

44. Xu, J., Simon, M.I., and Chen, J. Generation Of Rod Arrestin Knock-out Mice. 1996; Invest.Ophthalmol.Vis.Sci. S216
Goto Top

45. Yamaki, K., Tsuda, M., Kikuchi, T., Chen, K.H., Huang, K.P., and Shinohara, T. Structural organization of the human S-antigen gene. cDNA, amino acid, intron, exon, promoter, in vitro transcription, retina, and pineal gland. 1990; J.Biol.Chem. 265: 20757 - 20762.
Goto Top Link to PudMed

46. Yamaki, K., Tsuda, M., and Shinohara, T. The sequence of human retinal S-antigen reveals similarities with alpha-transducin. 1988; FEBS Letters. 234: 39 - 43.
Goto Top Link to PudMed

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