Dynamic Behavior of Rod Photoreceptor Disks

Chen, Chunhe; Yun-Hai, Jiang; Koutalos, Yiannis

doi:10.1016/s0006-3495(02)73911-8

Cited by 32 publications

(33 citation statements)

References 47 publications

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“…These results further illustrate that when Arr1 expression is absent in the retina, the synaptic activity is dramatically reduced in the photoreceptors. We also observed FM1-43 staining in the outer segment (Choi et al, 2005) in WT retinas and this staining pattern may indicate the continuous renewal process of the outer segment and dynamic communication of the disc and extracellular space(Chen et al, 2002). …”

Section: Resultsmentioning

confidence: 61%

Visual Arrestin 1 Acts As a Modulator for N-Ethylmaleimide-Sensitive Factor in the Photoreceptor Synapse

Huang¹,

Brown²,

Craft³

2010

Journal of Neuroscience

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In the G-protein-coupled receptor phototransduction cascade, visual Arrestin 1 (Arr1) binds to and deactivates phosphorylated light-activated opsins, a process that is critical for effective recovery and normal vision. In this report, we discovered a novel synaptic interaction between Arr1 and N-ethylmaleimide-sensitive factor (NSF) that is enhanced in a dark environment when mouse photoreceptors are depolarized and the rate of exocytosis is elevated. In the photoreceptor synapse, NSF functions to sustain a higher rate of exocytosis, in addition to the compensatory endocytosis to retrieve and to recycle vesicle membrane and synaptic proteins. Not only does Arr1 bind to the junction of NSF N-terminal and its first ATPase domains in an ATP-dependent manner in vitro, but Arr1 also enhances both NSF ATPase and NSF disassembly activities. In in vivo experiments in mouse retinas with the Arr1 gene knocked out, the expression levels of NSF and other synapse-enriched components, including vGLUT1 (vesicular glutamate transporter 1), EAAT5 (excitatory amino acid transporter 5), and VAMP2 (vesicle-associated membrane protein 2), are markedly reduced, which leads to a substantial decrease in the exocytosis rate with FM1-43. Thus, we propose that the Arr1 and NSF interaction is important for modulating normal synaptic function in mouse photoreceptors. This study demonstrates a vital alternative function for Arr1 in the photoreceptor synapse and provides key insights into the potential molecular mechanisms of inherited retinal diseases, such as Oguchi disease and Arr1-associated retinitis pigmentosa.

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Section: Resultsmentioning

confidence: 61%

Visual Arrestin 1 Acts As a Modulator for N-Ethylmaleimide-Sensitive Factor in the Photoreceptor Synapse

Huang¹,

Brown²,

Craft³

2010

Journal of Neuroscience

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“…Such data reveal that rod discs, which are closed to the cytoplasm (Chen et al, 2002), occupy about 50% of the envelope volume in the 'core' of the OS. Thus, the hypothesis predicts that fluorescence in the OS core should be about 50% of the maximal fluorescence in the rod.…”

Section: Analysis Of the Spatial Distribution Of Egfp In Individual Rodsmentioning

confidence: 96%

Quantification of the cytoplasmic spaces of living cells with EGFP reveals arrestin-EGFP to be in disequilibrium in dark adapted rod photoreceptors

Peet

Bragin

Calvert

et al. 2004

Journal of Cell Science

101

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The hypothesis is tested that enhanced green fluorescent protein (EGFP) can be used to quantify the aqueous spaces of living cells, using as a model transgenic Xenopus rods. Consistent with the hypothesis, regions of rods having structures that exclude EGFP, such as the mitochondrial-rich ellipsoid and the outer segments, have highly reduced EGFP fluorescence. Over a 300-fold range of expression the average EGFP concentration in the outer segment was approximately half that in the most intensely fluorescent regions of the inner segment, in quantitative agreement with prior X-ray diffraction estimates of outer segment cytoplasmic volume. In contrast, the fluorescence of soluble arrestin-EGFP fusion protein in the dark adapted rod outer segment was approximately threefold lower than predicted by the EGFP distribution, establishing that the fusion protein is not equilibrated with the cytoplasm. Arrestin-EGFP mass was conserved during a large-scale, light-driven redistribution in which ∼40% of the protein in the inner segment moved to the outer segment in less than 30 minutes.

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“…To determine the intracellular pH of rod outer segments, BCECF, a ratiometric pH-sensitive dye was used, following published procedures used with isolated salamander rod photoreceptors (13). Isolated mouse rod photoreceptors were incubated with 10 M BCECF-AM for 30 min, followed by washes with Ringer's to remove remaining extracellular dye.…”

Section: Animals-wild Type (129/sv) and Rpe65mentioning

confidence: 99%

Mitochondria Contribute to NADPH Generation in Mouse Rod Photoreceptors

Adler

Chen

Koutalos

2014

Journal of Biological Chemistry

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Background:The major source of NADPH is considered to be the pentose phosphate pathway. Results: In isolated mouse rod photoreceptors, blocking metabolite entry into mitochondria substantially reduces NADPH generation. Mitochondrial metabolic substrates support NADPH generation. Conclusion: Mitochondria-linked pathways contribute substantially to NADPH generation in mouse rod photoreceptors. Significance: A wide range of photoreceptor cell functions depend on adequate NADPH supply.

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Dynamic Behavior of Rod Photoreceptor Disks

Cited by 32 publications

References 47 publications

Visual Arrestin 1 Acts As a Modulator for N-Ethylmaleimide-Sensitive Factor in the Photoreceptor Synapse

Visual Arrestin 1 Acts As a Modulator for N-Ethylmaleimide-Sensitive Factor in the Photoreceptor Synapse

Quantification of the cytoplasmic spaces of living cells with EGFP reveals arrestin-EGFP to be in disequilibrium in dark adapted rod photoreceptors

Mitochondria Contribute to NADPH Generation in Mouse Rod Photoreceptors

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