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Open AccessArticle

Lack of a Retinal Phenotype in a Syne-2/Nesprin-2 Knockout Mouse Model

1
Animal Physiology, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany
2
Department of Ophthalmology, University Hospital Erlangen, 91054 Erlangen, Germany
3
Institute of Biochemistry I; Medical Faculty, University Hospital, University of Cologne, 50931 Cologne, Germany
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Cells 2019, 8(10), 1238; https://doi.org/10.3390/cells8101238
Received: 17 September 2019 / Revised: 4 October 2019 / Accepted: 10 October 2019 / Published: 11 October 2019
Syne-2 (also known as Nesprin-2) is a member of a family of proteins that are found primarily in the outer nuclear membrane, as well as other subcellular compartments. Syne-2 contains a C-terminal KASH transmembrane domain and is part of a protein network that associates the nuclear envelope to the cytoskeleton via the binding to actin filaments. Syne-2 plays a role in nuclear migration, nuclear positioning during retinal development, and in ciliogenesis. In a previous study, we showed a connection between Syne-2 and the multifunctional scaffold protein Pericentrin (Pcnt). The elimination of the interaction of Syne-2 and Pcnt showed defects in nuclear migration and the formation of outer segments during retinal development, as well as disturbances in centrosomal migration at the beginning of ciliogenesis in general. In this study, the Syne-2 KO mouse model Nesprin-2△ABD (Syne-2tm1Ngl, MGI) with special attention to Pcnt and ciliogenesis was analyzed. We show reduced expression of Syne-2 in the retina of the Syne-2 KO mouse but found no significant structural—and only a minor functional—phenotype. For the first time, detailed expression analyses showed an expression of a Syne-2 protein larger than 400 kDa (~750 kDa) in the Syne-2/Nesprin-2 KO mouse. In conclusion, the lack of an overt phenotype in Syne-2/Nesprin-2 KO mice suggests the usage of alternative translational start sites, producing Syne-2 splice variants with an intact Pcnt interaction site. Nevertheless, deletion of the actin-binding site in the Syne-2/Nesprin-2 KO mouse revealed a high variability in scotopic oscillatory potentials assuming a novel function of Syne-2 in synchronizing inner retinal processes. View Full-Text
Keywords: Syne-2; Pericentrin; retina; nuclear migration; primary cilium; ciliogenesis Syne-2; Pericentrin; retina; nuclear migration; primary cilium; ciliogenesis
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Falk, N.; Joachimsthaler, A.; Kessler, K.; Lux, U.T.; Noegel, A.A.; Kremers, J.; Brandstätter, J.H.; Gießl, A. Lack of a Retinal Phenotype in a Syne-2/Nesprin-2 Knockout Mouse Model. Cells 2019, 8, 1238.

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