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RanGTPase regulates the interaction between the inner nuclear membrane proteins, Samp1 and Emerin
Stockholm University, Faculty of Science, Department of Neurochemistry.
Stockholm University, Faculty of Science, Department of Neurochemistry.
Stockholm University, Faculty of Science, Department of Neurochemistry.
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Number of Authors: 62018 (English)In: Biochimica et Biophysica Acta - Biomembranes, ISSN 0005-2736, E-ISSN 1879-2642, Vol. 1860, no 6, p. 1326-1334Article in journal (Refereed) Published
Abstract [en]

Samp1, spindle associated membrane protein 1, is a type II integral membrane protein localized in the inner nuclear membrane. Recent studies have shown that the inner nuclear membrane protein, Emerin and the small monomeric GTPase, Ran are direct binding partners of Samp1. Here we addressed the question whether Ran could regulate the interaction between Samp1 and Emerin in the inner nuclear membrane. To investigate the interaction between Samp1 and Emerin in live cells, we performed FRAP experiments in cells overexpressing YFP-Emerin. We compared the mobility of YFP-Emerin in Samp1 knock out cells and cells overexpressing Samp1. The results showed that the mobility of YFP-Emerin was higher in Samp1 knock out cells and lower in cells overexpressing Samp1, suggesting that Samp1 significantly attenuates the mobility of Emerin in the nuclear envelope. FRAP experiments using tsBN2 cells showed that the mobility of Emerin depends on RanGTP. Consistently, in vitro binding experiments showed that the affinity between Samp1 and Emerin is decreased in the presence of Ran, suggesting that Ran attenuates the interaction between Samp1 and Emerin. This is the first demonstration that Ran can regulate the interaction between two proteins in the nuclear envelope.

Place, publisher, year, edition, pages
2018. Vol. 1860, no 6, p. 1326-1334
Keywords [en]
Muscular dystrophy, Nuclear membrane, Samp1, Emerin, Ran, FRAP
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-157708DOI: 10.1016/j.bbamem.2018.03.001ISI: 000432758400009PubMedID: 29510091OAI: oai:DiVA.org:su-157708DiVA, id: diva2:1236181
Available from: 2018-07-31 Created: 2018-07-31 Last updated: 2018-07-31Bibliographically approved

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Vijayaraghavan, BalajeFigueroa, Ricardo A.Bergqvist, CeciliaHallberg, Einar
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