Please use this identifier to cite or link to this item: doi:10.22028/D291-36723
Title: Ciliary Proteins Repurposed by the Synaptic Ribbon: Trafficking Myristoylated Proteins at Rod Photoreceptor Synapses
Author(s): Suiwal, Shweta
Dembla, Mayur
Schwarz, Karin
Katiyar, Rashmi
Jung, Martin
Carius, Yvonne
Maxeiner, Stephan
Lauterbach, Marcel A.
Lancaster, C. Roy D.
Schmitz, Frank
Language: English
Title: International Journal of Molecular Sciences
Volume: 23
Issue: 13
Publisher/Platform: MDPI
Year of Publication: 2022
Free key words: retina
photoreceptor synapse
synaptic ribbon
Nphp3
Arl3
Arl13b
immunogold electron microscopy
DDC notations: 610 Medicine and health
Publikation type: Journal Article
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 of the first publication: 10.3390/ijms23137135
Link to this record: urn:nbn:de:bsz:291--ds-367236
hdl:20.500.11880/33373
http://dx.doi.org/10.22028/D291-36723
ISSN: 1422-0067
Date of registration: 8-Jul-2022
Description of the related object: Supplementary Materials
Related object: https://www.mdpi.com/article/10.3390/ijms23137135/s1
Faculty: M - Medizinische Fakultät
Department: M - Anatomie und Zellbiologie
M - Biophysik
M - Medizinische Biochemie und Molekularbiologie
Professorship: M - Prof. Dr. C. Roy D. Lancaster
M - Jun.-Prof. Dr. Marcel Lauterbach
M - Prof. Dr. Frank Schmitz
Collections:SciDok - Der Wissenschaftsserver der Universität des Saarlandes

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