Mutation Associated with an Autosomal Dominant Cone-Rod Dystrophy CORD7 Modifies RIM1-Mediated Modulation of Voltage-Dependent Ca2+ Channels

@article{Miki2007MutationAW,
  title={Mutation Associated with an Autosomal Dominant Cone-Rod Dystrophy CORD7 Modifies RIM1-Mediated Modulation of Voltage-Dependent Ca2+ Channels},
  author={Takafumi Miki and Shigeki Kiyonaka and Yoshitsugu Uriu and Michel De Waard and Minoru Wakamuri and Kevin P Campbell and Yasou Mori},
  journal={Channels},
  year={2007},
  volume={1},
  pages={144 - 147 - 701}
}
Genetic analyses have revealed an association between the gene encoding the Rab3A‑interacting molecule (RIM1) and the autosomal dominant cone‑rod dystrophy CORD7. However, the pathogenesis of CORD7 remains unclear. We recently revealed that RIM1 regulates voltage‑dependent Ca2+ channel (VDCC) currents and anchors neurotransmitter‑containing vesicles to VDCCs, thereby controlling neurotransmitter release. We demonstrate here that the mouse RIM1 arginine‑to‑histidine substitution (R655H), which… 
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TLDR
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TLDR
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TLDR
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Loss of Function of RIMS2 Causes a Syndromic Congenital Cone-Rod Synaptic Disease with Neurodevelopmental and Pancreatic Involvement
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Functional Coupling of Rab3-interacting Molecule 1 (RIM1) and L-type Ca2+ Channels in Insulin Release*
TLDR
A novel functional coupling between RIM1 and the L-type CaV channels via the CaVβ auxiliary subunit that contribute to determine insulin secretion is unveiled.
Rim1 modulates direct G-protein regulation of Cav2.2 channels
TLDR
The data suggest that Rim1-induced facilitation of neurotransmitter release may come as a consequence of a decrease in the inhibitory pathway carried by G-proteins that contributes, together with the slowing of channel inactivation, to maintain Ca2+ influx under prolonged activity.
Causes and consequences of inherited cone disorders
TLDR
Future research will aim to elucidate the remaining causative genes, identify the molecular mechanisms of CD, and develop novel therapies aimed at preventing vision loss in individuals with CD in the future.
RIM genes differentially contribute to organizing presynaptic release sites
TLDR
It is found that although the RIM2 C2B domain by itself significantly decreased Ca2+-channel inactivation in transfected HEK293 cells, it did not rescue any aspect of the Rims knockout phenotype in cultured neurons, suggesting that RIMs primarily act in release as physical Ca2-channel tethers and not as Ca2+,-channel modulators.
Functional interactions between voltage-gated Ca(2+) channels and Rab3-interacting molecules (RIMs): new insights into stimulus-secretion coupling.
TLDR
Recent evidences are reviewed providing support for the notion that RIMs directly bind to the pore-forming and auxiliary β subunits of Ca(V) channels and with RIM-binding protein, another interactor of the channels, significantly influencing hormone and neurotransmitter release.
Presynaptic [Ca2+] and GCAPs: aspects on the structure and function of photoreceptor ribbon synapses
  • F. Schmitz
  • Biology, Medicine
    Front. Mol. Neurosci.
  • 2014
TLDR
This review focuses on the regulation of [Ca2+] in presynaptic photoreceptor terminals and on the function of a particular Ca2+-regulated protein, the neuronal calcium sensor protein GCAP2 (guanylate cyclase-activating protein-2) in the photoreceptors' ribbon synapse.
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TLDR
A mutation has been identified in the Rab3A-interacting molecule (RIM1) gene in CORD7, an autosomal dominant cone-rod dystrophy that localises to chromosome 6q14, indicating that it is not a common polymorphism, and the almost complete sequence conservation of the C(2)A domain between human and rat RIM1 is consistent with a disease role for the change.
Loss-of-function mutations in a calcium-channel α1-subunit gene in Xp11.23 cause incomplete X-linked congenital stationary night blindness
TLDR
It is established that loss-of-function mutations in CACNA1F cause incomplete CSNB, making this disorder an example of a human channelopathy of the retina.
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TLDR
Immunohistochemical analyses show that Cav1.4 is widely distributed outside the retina, including in the immune system, thus suggesting a broader role in human physiology, and the channel is ideally suited for tonic calcium influx at typical photoreceptor resting potentials.
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TLDR
RIM1 association with β in the presynaptic active zone supports release via two distinct mechanisms: sustaining Ca2+ influx through inhibition of channel inactivation, and anchoring neurotransmitter-containing vesicles in the vicinity of VDCCs.
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TLDR
The findings suggest that genetic mutation may enhance human cognition in some cases and a possible role for RIMS1 in the enhancement of cognitive function at least in this kindred is suggested.
Redundant functions of RIM1α and RIM2α in Ca2+‐triggered neurotransmitter release
TLDR
It is found that deletion of either RIM1α or RIM2α is not lethal, but ablation of both α‐RIMs causes postnatal death, and α‐ RIMs are not essential for synapse formation or synaptic exocytosis, but are required for normal Ca2+‐triggering of exocyTosis.
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TLDR
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Cav1.4α1 Subunits Can Form Slowly Inactivating Dihydropyridine-Sensitive L-Type Ca2+ Channels Lacking Ca2+-Dependent Inactivation
TLDR
The biophysical and pharmacological properties of human retinal Cav1.4α1 + α2δ1 + β channel complexes can form LTCCs with intermediate DHP antagonist sensitivity lacking Ca2+-dependent inactivation, and their biophysical properties should enable them to contribute to sustained ICa,L at negative potentials.
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TLDR
A novel CAZ protein of approximately 120 kD from rat brain is identified and named CAST (CAZ-associated structural protein), which had no transmembrane segment, but had four coiled-coil domains and a putative COOH-terminal consensus motif for binding to PDZ domains.
Direct Interaction of the Rab3 Effector RIM with Ca2+Channels, SNAP-25, and Synaptotagmin*
TLDR
It is proposed that the Rab3 effector RIM is a scaffold protein that participates through its multiple binding partners in the docking and fusion of secretory vesicles at the release sites.
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