Developmental localization of adhesion and scaffolding proteins at the cone synapse

Nuhn, John S.; Fuerst, Peter G.

doi:10.1016/j.gep.2014.07.003

Cited by 8 publications

(5 citation statements)

References 42 publications

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“…Finally, the MAGUK family member Calcium/Calmodulin-Dependent Serine Protein Kinase (CASK) was abundantly present throughout the IPL ( Figure 1E ) and present in dense blobs consistent with photoreceptor terminals in the OPL ( Figure 1F ). This is consistent with previous studies demonstrating its presence in photoreceptor terminals ( Nuhn and Fuerst, 2014 ). Note that antibodies to PSD95 and CASK used were mouse antibodies, so labeling of blood vessels in Figures 1A,E (examples marked with asterisks) is a non-specific result of secondary antibody binding.…”

Section: Resultssupporting

confidence: 94%

Synaptic Scaffolds, Ion Channels and Polyamines in Mouse Photoreceptor Synapses: Anatomy of a Signaling Complex

Vila

Shihabeddin

Zhang

et al. 2021

Front. Cell. Neurosci.

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Synaptic signaling complexes are held together by scaffold proteins, each of which is selectively capable of interacting with a number of other proteins. In previous studies of rabbit retina, we found Synapse-Associated Protein-102 (SAP102) and Channel Associated Protein of Synapse-110 (Chapsyn110) selectively localized in the tips of horizontal cell processes at contacts with rod and cone photoreceptors, along with several interacting ion channels. We have examined the equivalent suites of proteins in mouse retina and found similarities and differences. In the mouse retina we identified Chapsyn110 as the scaffold selectively localized in the tips of horizontal cells contacting photoreceptors, with Sap102 more diffusely present. As in rabbit, the inward rectifier potassium channel Kir2.1 was present with Chapsyn110 on the tips of horizontal cell dendrites within photoreceptor invaginations, where it could provide a hyperpolarization-activated current that could contribute to ephaptic signaling in the photoreceptor synapses. Pannexin 1 and Pannexin 2, thought to play a role in ephaptic and/or pH mediated signaling, were present in the outer plexiform layer, but likely not in the horizontal cells. Polyamines regulate many ion channels and control the degree of rectification of Kir2.1 by imposing a voltage-dependent block. During the day polyamine immunolabeling was unexpectedly high in photoreceptor terminals compared to other areas of the retina. This content was significantly lower at night, when polyamine content was predominantly in Müller glia, indicating daily rhythms of polyamine content. Both rod and cone terminals displayed the same rhythm. While polyamine content was not prominent in horizontal cells, if polyamines are released, they may regulate the activity of Kir2.1 channels located in the tips of HCs. The rhythmic change in polyamine content of photoreceptor terminals suggests that a daily rhythm tunes the behavior of suites of ion channels within the photoreceptor synapses.

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Section: Resultssupporting

confidence: 94%

Synaptic Scaffolds, Ion Channels and Polyamines in Mouse Photoreceptor Synapses: Anatomy of a Signaling Complex

Vila

Shihabeddin

Zhang

et al. 2021

Front. Cell. Neurosci.

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“…Subcellular fractionation and microscopic imaging studies have shown that isoforms of Pcdhα and Pcdhγ are located at synaptic junctions ( Kohmura et al, 1998 ; Wang et al, 2002b ; Phillips et al, 2003 ; Lefebvre et al, 2008 ; Garrett and Weiner, 2009 ). In addition, two isoforms of Pcdhβ, β16 and β22, have been found to be enriched in subsets of synapses in the retina and cerebellum ( Junghans et al, 2008 ; Puller and Haverkamp, 2011 ; Nuhn and Fuerst, 2014 ). Finally, isoforms of Pcdhγ are found to accumulate at axodendritic and dendrodendritic synapses ( Fernandez-Monreal et al, 2009 ).…”

Section: Biological Functions Of Clustered Pcdhsmentioning

confidence: 99%

Clustered Protocadherins Emerge as Novel Susceptibility Loci for Mental Disorders

Jia

2020

Front. Neurosci.

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The clustered protocadherins (cPcdhs) are a subfamily of type I single-pass transmembrane cell adhesion molecules predominantly expressed in the brain. Their stochastic and combinatorial expression patterns encode highly diverse neural identity codes which are central for neuronal self-avoidance and non-self discrimination in brain circuit formation. In this review, we first briefly outline mechanisms for generating a tremendous diversity of cPcdh cell-surface assemblies. We then summarize the biological functions of cPcdhs in a wide variety of neurodevelopmental processes, such as neuronal migration and survival, dendritic arborization and self-avoidance, axonal tiling and even spacing, and synaptogenesis. We focus on genetic, epigenetic, and 3D genomic dysregulations of cPcdhs that are associated with various neuropsychiatric and neurodevelopmental diseases. A deeper understanding of regulatory mechanisms and physiological functions of cPcdhs should provide significant insights into the pathogenesis of mental disorders and facilitate development of novel diagnostic and therapeutic strategies.

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“…This is known to be an early event in the formation of functional synapses between developing photoreceptors and second-order neurons in the neurosensory retina. 32 The two key proteins in photoreceptor ribbon synapse formation are BASSOON and RIBEYE. 33 Immunohistochemical localization of BASSOON and RIBEYE proteins demonstrated noteworthy expression in transplanted PPCs after just 4 days (Fig.…”

Section: Fig 3 Confocal Images Of Ppcsmentioning

confidence: 99%

“…32 In the rodent, this is initiated at about P6 and is completed when the eyes open at P14. 38 The assembly of photoreceptor ribbon synapses involves the formation and trafficking of sphere-like protein aggregates of the ribbon matrix proteins BASSOON, RIBEYE, Piccolo, and RIM1.…”

mentioning

confidence: 99%

Enhanced Functional Integration of Human Photoreceptor Precursors into Human and Rodent Retina in anEx VivoRetinal Explant Model System

Yanai

Laver

Gregory‐Evans

et al. 2015

Tissue Engineering Part A

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Retinal disease is the major cause of irreversible blindness in developed countries. Transplantation of photoreceptor precursor cells (PPCs) derived from human embryonic stem cells (hESCs) is a promising and widely applicable approach for the treatment of these blinding conditions. Previously, it has been shown that after transplantation into the degenerating retina, the percentage of PPCs that undergo functional integration is low. The factors that inhibit PPC engraftment remain largely unknown, in part, because so many adverse factors could be at play during in vivo experiments. To advance our knowledge in overcoming potential adverse effects and optimize PPC transplantation, we have developed a novel ex vivo system. Harvested neural retina was placed directly on top of cultured retinal pigment epithelial (RPE) cells from a number of different sources. To mimic PPC transplantation into the subretinal space, hESC-derived PPCs were inserted between the retinal explant and underlying RPE. Explants cocultured with hESC-derived RPE maintained normal gross morphology and viability for up to 2 weeks, whereas the explants cultured on ARPE19 and RPE-J failed by 7 days. Furthermore, the proportion of PPCs expressing ribbon synapse-specific proteins BASSOON and RIBEYE was significantly higher when cocultured with hESC-derived RPE (20% and 10%, respectively), than when cocultured with ARPE19 (only 6% and 2%, respectively). In the presence of the synaptogenic factor thrombospondin-1 (TSP-1), the proportion of BASSOON-positive and RIBEYE-positive PPCs cocultured with hESC-derived RPE increased to *30% and 15%, respectively. These data demonstrate the utility of an ex vivo model system to define factors, such as TSP-1, which could influence integration efficiency in future in vivo experiments in models of retinal degeneration.

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Developmental localization of adhesion and scaffolding proteins at the cone synapse

Cited by 8 publications

References 42 publications

Synaptic Scaffolds, Ion Channels and Polyamines in Mouse Photoreceptor Synapses: Anatomy of a Signaling Complex

Synaptic Scaffolds, Ion Channels and Polyamines in Mouse Photoreceptor Synapses: Anatomy of a Signaling Complex

Clustered Protocadherins Emerge as Novel Susceptibility Loci for Mental Disorders

Enhanced Functional Integration of Human Photoreceptor Precursors into Human and Rodent Retina in anEx VivoRetinal Explant Model System

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