Transient, cyclic changes in mouse visual cell gene products during the light‐dark cycle

McGinnis, James F.; Whelan, James P.; Donoso, Larry A.

doi:10.1002/jnr.490310325

Cited by 102 publications

(49 citation statements)

References 21 publications

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“…1, 15 min, 60 min light). This pattern of arrestin immunoreactivity and the time course of arrestin translocation were similar to previous reports (Philp et al, 1987;Mangini and Pepperberg, 1988;Whelan and McGinnis, 1988;McGinnis et al, 1992).…”

Section: Light Causes Arrestin Translocation In the Absence Of Rhodopsupporting

confidence: 92%

“…Light triggers a massive movement of transducin to the rod inner segment in the opposite direction from arrestin (Brann and Cohen, 1987;Philp et al, 1987;Whelan and McGinnis, 1988;Organisciak et al, 1991;McGinnis et al, 1992;Sokolov et al, 2002). We showed that arrestin translocation was unaffected in the absence of Tr ␣ .…”

Section: Arrestin and Transducin Translocation In Retinal Rods Are Inmentioning

confidence: 77%

“…Arrestin immunostaining predominates at rod inner segments, the outer nuclear layer, and the outer plexiform layer of dark-adapted retinas, shifting to rod outer segments during light exposure. Immunoreactivity of the transducin ␣ and ␤ subunits shifts in the opposite direction in response to light (Philp et al, 1987;Whelan and McGinnis, 1988;McGinnis et al, 1992). Recently, Sokolov et al (2002) confirmed the physiological movement of transducin by combining serial tangential cryosectioning of the retina with Western blot analysis and demonstrated that this movement extends the range of light intensities in which the rods can operate.…”

Section: Introductionmentioning

confidence: 94%

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Light-Dependent Translocation of Arrestin in the Absence of Rhodopsin Phosphorylation and Transducin Signaling

2003

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Visual arrestin plays a crucial role in the termination of the light response in vertebrate photoreceptors by binding selectively to lightactivated, phosphorylated rhodopsin. Arrestin localizes predominantly to the inner segments and perinuclear region of dark-adapted rod photoreceptors, whereas light induces redistribution of arrestin to the rod outer segments. The mechanism by which arrestin redistributes in response to light is not known, but it is thought to be associated with the ability of arrestin to bind photolyzed, phosphorylated rhodopsin in the outer segment. In this study, we show that light-driven translocation of arrestin is unaffected in two different mouse models in which rhodopsin phosphorylation is lacking. We further show that arrestin movement is initiated by rhodopsin but does not require transducin signaling. These results exclude passive diffusion and point toward active transport as the mechanism for lightdependent arrestin movement in rod photoreceptor cells.

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Section: Light Causes Arrestin Translocation In the Absence Of Rhodopsupporting

confidence: 92%

Section: Arrestin and Transducin Translocation In Retinal Rods Are Inmentioning

confidence: 77%

Section: Introductionmentioning

confidence: 94%

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Light-Dependent Translocation of Arrestin in the Absence of Rhodopsin Phosphorylation and Transducin Signaling

2003

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“…9B. Arrestin was present predominantly in the inner segments of photoreceptors of dark-adapted retinas but was present only in the outer segment of light-adapted retinas, in agreement with previous reports (22). The translocation of arrestin between the inner and outer segments is quite evident; however, Src shows only differences in the intensity of reaction and not localization in response to light.…”

Section: Light-induced Tyrosine Phosphorylation Of Ros-supporting

confidence: 91%

Light-dependent Association of Src with Photoreceptor Rod Outer Segment Membrane Proteinsin Vivo

Ghalayini¹,

Desai²,

Smith³

et al. 2002

Journal of Biological Chemistry

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In vivo light exposure results in tyrosine phosphorylation of several rod outer segment (ROS) proteins (Ghalayini, A. J., Guo, X. X., Koutz, C. A, and Anderson, R. E. (1998) Exp. Eye Res. 66, 817-821). We now report the presence of Src in ROS and its increased association with bleached ROS membranes. Immunoprecipitation with anti-phosphotyrosine revealed that tyrosine kinase activity recovered from light-adapted ROS membranes was twice that recovered from dark-adapted ROS. Other experiments revealed the presence of both bleached rhodopsin and arrestin in immunoprecipitates of LROS, suggesting the formation of a multimeric complex containing Src, arrestin, and bleached rhodopsin. Additionally, when immobilized Src homology domains 2 and 3 (SH2 and SH3, respectively) were used to study the association of Src with ROS membranes, only bleached opsin and arrestin were found to associate with the SH2 domain of Src. These data strongly suggest that Src through its SH2 domain interacts with bleached rhodopsin and arrestin either directly or indirectly. Similar results were also obtained when dark-adapted and light-adapted retinas were used instead of ROS membranes. Our data strongly suggest that light exposure in vivo activates Src and promotes its association through its SH2 domain with a complex containing bleached rhodopsin and arrestin. A hypothesis for the functional significance of this phenomenon is presented.Tyrosine phosphorylation plays an important role in many cellular functions including growth, development, proliferation, and survival. Several extracellular signals including insulin, growth factors, mitogens, and others produce their intracellular effects through the activation of the appropriate receptor tyrosine kinases or nonreceptor protein-tyrosine kinases (1). This activation results in tyrosine phosphorylation of key intracellular proteins that are either enzymes or play the role of adaptor proteins between other intracellular signaling proteins (2). In the case of receptor tyrosine kinases, receptor activation causes a rapid autophosphorylation on tyrosine residues, which leads to association of these receptors with key intracellular proteins, resulting in tyrosine phosphorylation of these target proteins. Among the enzymes that are tyrosinephosphorylated upon activation are Ras-GTPase-activating protein, phospholipase C␥ (PLC␥), 1 phosphatidylinositol 3-kinase, protein-tyrosine phosphatases including the ubiquitous SHP-2, and a growing list of other enzymes (2-5).Although most of the current information regarding the biological significance of tyrosine phosphorylation involves receptor tyrosine kinases and nonreceptor protein-tyrosine kinases that are stimulated by growth factors and mitogens, there is recent evidence indicating the involvement of G-protein-coupled receptors (GPCRs) in the generation of tyrosine phosphorylation-based signals (for a recent review, see Ref. 6). One such example is the angiotensin II receptor (AT 1 ), a seventransmembrane receptor with no intrinsic kinase activity, w...

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“…The onset of rod arrestin gene transcription in mouse occurs before rod outer segment formation (27), whereas in the bovine retina, arrestin expression is concurrent with other genes involved in phototransduction (28). Transcription of arrestin also appears to be regulated by diurnal or circadian rhythms in certain species (29,30,31). However, the mechanisms that control arrestin expression are not understood.…”

mentioning

confidence: 99%

Immediate Upstream Sequence of Arrestin Directs Rod-specific Expression in Xenopus

Mani

Besharse

Knox

1999

Journal of Biological Chemistry

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Transient, cyclic changes in mouse visual cell gene products during the light‐dark cycle

Cited by 102 publications

References 21 publications

Light-Dependent Translocation of Arrestin in the Absence of Rhodopsin Phosphorylation and Transducin Signaling

Light-Dependent Translocation of Arrestin in the Absence of Rhodopsin Phosphorylation and Transducin Signaling

Light-dependent Association of Src with Photoreceptor Rod Outer Segment Membrane Proteinsin Vivo

Immediate Upstream Sequence of Arrestin Directs Rod-specific Expression in Xenopus

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