Association of shank 1A scaffolding protein with cone photoreceptor terminals in the mammalian retina.

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Association of shank 1A scaffolding protein with cone photoreceptor terminals in the mammalian retina. / Stella, Salvatore L; Vila, Alejandro; Hung, Albert Y; Rome, Michael E; Huynh, Uyenchi; Sheng, Morgan; Kreienkamp, Hans-Jürgen; Brecha, Nicholas C.

in: PLOS ONE, Jahrgang 7, Nr. 9, 9, 2012, S. 43463.

Publikationen: SCORING: Beitrag in Fachzeitschrift/ZeitungSCORING: ZeitschriftenaufsatzForschungBegutachtung

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APA

Stella, S. L., Vila, A., Hung, A. Y., Rome, M. E., Huynh, U., Sheng, M., Kreienkamp, H-J., & Brecha, N. C. (2012). Association of shank 1A scaffolding protein with cone photoreceptor terminals in the mammalian retina. PLOS ONE, 7(9), 43463. [9]. https://doi.org/10.1371/journal.pone.0043463

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Bibtex

@article{f41c7e54c08d4b5294e22b75ca527801,
title = "Association of shank 1A scaffolding protein with cone photoreceptor terminals in the mammalian retina.",
abstract = "Photoreceptor terminals contain post-synaptic density (PSD) proteins e.g., PSD-95/PSD-93, but their role at photoreceptor synapses is not known. PSDs are generally restricted to post-synaptic boutons in central neurons and form scaffolding with multiple proteins that have structural and functional roles in neuronal signaling. The Shank family of proteins (Shank 1-3) functions as putative anchoring proteins for PSDs and is involved in the organization of cytoskeletal/signaling complexes in neurons. Specifically, Shank 1 is restricted to neurons and interacts with both receptors and signaling molecules at central neurons to regulate plasticity. However, it is not known whether Shank 1 is expressed at photoreceptor terminals. In this study we have investigated Shank 1A localization in the outer retina at photoreceptor terminals. We find that Shank 1A is expressed presynaptically in cone pedicles, but not rod spherules, and it is absent from mice in which the Shank 1 gene is deleted. Shank 1A co-localizes with PSD-95, peanut agglutinin, a marker of cone terminals, and glycogen phosphorylase, a cone specific marker. These findings provide convincing evidence for Shank 1A expression in both the inner and outer plexiform layers, and indicate a potential role for PSD-95/Shank 1 complexes at cone synapses in the outer retina.",
keywords = "Animals, Mice, Mice, Inbred C57BL, Gene Deletion, Mice, Transgenic, Protein Binding, Organ Specificity, Nerve Tissue Proteins/*metabolism, Membrane Proteins/metabolism, Guanylate Kinase/metabolism, Mammals/*metabolism, Peanut Agglutinin/metabolism, Retinal Cone Photoreceptor Cells/cytology/*metabolism, Synapses/metabolism, Wheat Germ Agglutinins/metabolism, Animals, Mice, Mice, Inbred C57BL, Gene Deletion, Mice, Transgenic, Protein Binding, Organ Specificity, Nerve Tissue Proteins/*metabolism, Membrane Proteins/metabolism, Guanylate Kinase/metabolism, Mammals/*metabolism, Peanut Agglutinin/metabolism, Retinal Cone Photoreceptor Cells/cytology/*metabolism, Synapses/metabolism, Wheat Germ Agglutinins/metabolism",
author = "Stella, {Salvatore L} and Alejandro Vila and Hung, {Albert Y} and Rome, {Michael E} and Uyenchi Huynh and Morgan Sheng and Hans-J{\"u}rgen Kreienkamp and Brecha, {Nicholas C}",
year = "2012",
doi = "10.1371/journal.pone.0043463",
language = "English",
volume = "7",
pages = "43463",
journal = "PLOS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "9",

}

RIS

TY - JOUR

T1 - Association of shank 1A scaffolding protein with cone photoreceptor terminals in the mammalian retina.

AU - Stella, Salvatore L

AU - Vila, Alejandro

AU - Hung, Albert Y

AU - Rome, Michael E

AU - Huynh, Uyenchi

AU - Sheng, Morgan

AU - Kreienkamp, Hans-Jürgen

AU - Brecha, Nicholas C

PY - 2012

Y1 - 2012

N2 - Photoreceptor terminals contain post-synaptic density (PSD) proteins e.g., PSD-95/PSD-93, but their role at photoreceptor synapses is not known. PSDs are generally restricted to post-synaptic boutons in central neurons and form scaffolding with multiple proteins that have structural and functional roles in neuronal signaling. The Shank family of proteins (Shank 1-3) functions as putative anchoring proteins for PSDs and is involved in the organization of cytoskeletal/signaling complexes in neurons. Specifically, Shank 1 is restricted to neurons and interacts with both receptors and signaling molecules at central neurons to regulate plasticity. However, it is not known whether Shank 1 is expressed at photoreceptor terminals. In this study we have investigated Shank 1A localization in the outer retina at photoreceptor terminals. We find that Shank 1A is expressed presynaptically in cone pedicles, but not rod spherules, and it is absent from mice in which the Shank 1 gene is deleted. Shank 1A co-localizes with PSD-95, peanut agglutinin, a marker of cone terminals, and glycogen phosphorylase, a cone specific marker. These findings provide convincing evidence for Shank 1A expression in both the inner and outer plexiform layers, and indicate a potential role for PSD-95/Shank 1 complexes at cone synapses in the outer retina.

AB - Photoreceptor terminals contain post-synaptic density (PSD) proteins e.g., PSD-95/PSD-93, but their role at photoreceptor synapses is not known. PSDs are generally restricted to post-synaptic boutons in central neurons and form scaffolding with multiple proteins that have structural and functional roles in neuronal signaling. The Shank family of proteins (Shank 1-3) functions as putative anchoring proteins for PSDs and is involved in the organization of cytoskeletal/signaling complexes in neurons. Specifically, Shank 1 is restricted to neurons and interacts with both receptors and signaling molecules at central neurons to regulate plasticity. However, it is not known whether Shank 1 is expressed at photoreceptor terminals. In this study we have investigated Shank 1A localization in the outer retina at photoreceptor terminals. We find that Shank 1A is expressed presynaptically in cone pedicles, but not rod spherules, and it is absent from mice in which the Shank 1 gene is deleted. Shank 1A co-localizes with PSD-95, peanut agglutinin, a marker of cone terminals, and glycogen phosphorylase, a cone specific marker. These findings provide convincing evidence for Shank 1A expression in both the inner and outer plexiform layers, and indicate a potential role for PSD-95/Shank 1 complexes at cone synapses in the outer retina.

KW - Animals

KW - Mice

KW - Mice, Inbred C57BL

KW - Gene Deletion

KW - Mice, Transgenic

KW - Protein Binding

KW - Organ Specificity

KW - Nerve Tissue Proteins/metabolism

KW - Membrane Proteins/metabolism

KW - Guanylate Kinase/metabolism

KW - Mammals/metabolism

KW - Peanut Agglutinin/metabolism

KW - Retinal Cone Photoreceptor Cells/cytology/metabolism

KW - Synapses/metabolism

KW - Wheat Germ Agglutinins/metabolism

KW - Animals

KW - Mice

KW - Mice, Inbred C57BL

KW - Gene Deletion

KW - Mice, Transgenic

KW - Protein Binding

KW - Organ Specificity

KW - Nerve Tissue Proteins/metabolism

KW - Membrane Proteins/metabolism

KW - Guanylate Kinase/metabolism

KW - Mammals/metabolism

KW - Peanut Agglutinin/metabolism

KW - Retinal Cone Photoreceptor Cells/cytology/metabolism

KW - Synapses/metabolism

KW - Wheat Germ Agglutinins/metabolism

U2 - 10.1371/journal.pone.0043463

DO - 10.1371/journal.pone.0043463

M3 - SCORING: Journal article

VL - 7

SP - 43463

JO - PLOS ONE

JF - PLOS ONE

SN - 1932-6203

IS - 9

M1 - 9

ER -