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doi:10.22028/D291-36723
Titel: | Ciliary Proteins Repurposed by the Synaptic Ribbon: Trafficking Myristoylated Proteins at Rod Photoreceptor Synapses |
VerfasserIn: | Suiwal, Shweta Dembla, Mayur Schwarz, Karin Katiyar, Rashmi Jung, Martin Carius, Yvonne Maxeiner, Stephan Lauterbach, Marcel A. Lancaster, C. Roy D. Schmitz, Frank |
Sprache: | Englisch |
Titel: | International Journal of Molecular Sciences |
Bandnummer: | 23 |
Heft: | 13 |
Verlag/Plattform: | MDPI |
Erscheinungsjahr: | 2022 |
Freie Schlagwörter: | retina photoreceptor synapse synaptic ribbon Nphp3 Arl3 Arl13b immunogold electron microscopy |
DDC-Sachgruppe: | 610 Medizin, Gesundheit |
Dokumenttyp: | Journalartikel / Zeitschriftenartikel |
Abstract: | The Unc119 protein mediates transport of myristoylated proteins to the photoreceptor outer segment, a specialized primary cilium. This transport activity is regulated by the GTPase Arl3 as well as by Arl13b and Rp2 that control Arl3 activation/inactivation. Interestingly, Unc119 is also enriched in photoreceptor synapses and can bind to RIBEYE, the main component of synaptic ribbons. In the present study, we analyzed whether the known regulatory proteins, that control the Unc119- dependent myristoylated protein transport at the primary cilium, are also present at the photoreceptor synaptic ribbon complex by using high-resolution immunofluorescence and immunogold electron microscopy. We found Arl3 and Arl13b to be enriched at the synaptic ribbon whereas Rp2 was predominantly found on vesicles distributed within the entire terminal. These findings indicate that the synaptic ribbon could be involved in the discharge of Unc119-bound lipid-modified proteins. In agreement with this hypothesis, we found Nphp3 (Nephrocystin-3), a myristoylated, Unc119- dependent cargo protein enriched at the basal portion of the ribbon in close vicinity to the active zone. Mutations in Nphp3 are known to be associated with Senior–Løken Syndrome 3 (SLS3). Visual impairment and blindness in SLS3 might thus not only result from ciliary dysfunctions but also from malfunctions of the photoreceptor synapse. |
DOI der Erstveröffentlichung: | 10.3390/ijms23137135 |
Link zu diesem Datensatz: | urn:nbn:de:bsz:291--ds-367236 hdl:20.500.11880/33373 http://dx.doi.org/10.22028/D291-36723 |
ISSN: | 1422-0067 |
Datum des Eintrags: | 8-Jul-2022 |
Bezeichnung des in Beziehung stehenden Objekts: | Supplementary Materials |
In Beziehung stehendes Objekt: | https://www.mdpi.com/article/10.3390/ijms23137135/s1 |
Fakultät: | M - Medizinische Fakultät |
Fachrichtung: | M - Anatomie und Zellbiologie M - Biophysik M - Medizinische Biochemie und Molekularbiologie |
Professur: | M - Prof. Dr. C. Roy D. Lancaster M - Jun.-Prof. Dr. Marcel Lauterbach M - Prof. Dr. Frank Schmitz |
Sammlung: | SciDok - Der Wissenschaftsserver der Universität des Saarlandes |
Dateien zu diesem Datensatz:
Datei | Beschreibung | Größe | Format | |
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ijms-23-07135.pdf | 9,3 MB | Adobe PDF | Öffnen/Anzeigen |
Diese Ressource wurde unter folgender Copyright-Bestimmung veröffentlicht: Lizenz von Creative Commons