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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

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