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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.
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(English)Manuscript (preprint) (Other (popular science, discussion, etc.))
National Category
Biological Sciences
Research subject
Neurochemistry with Molecular Neurobiology
Identifiers
URN: urn:nbn:se:su:diva-148431OAI: oai:DiVA.org:su-148431DiVA: diva2:1152372
Available from: 2017-10-24 Created: 2017-10-24 Last updated: 2017-10-30Bibliographically approved
In thesis
1. Identification and characterization of protein-protein interactions in the nuclear envelope
Open this publication in new window or tab >>Identification and characterization of protein-protein interactions in the nuclear envelope
2017 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The nuclear envelope forms the interface between the nucleus and the cytoplasm. The nuclear envelope consists of the two concentric lipid membranes, the nuclear pores and the nuclear lamina. The inner nuclear membrane contains hundreds of unique transmembrane proteins showing high tissue diversity. Mutations of some proteins in the nuclear envelope give rise to a broad spectrum of diseases called envelopathies or laminopathies. In this thesis, I aimed to study the functional organization of the nuclear envelope by identifying and characterizing interactions between the nuclear envelope proteins. For this, we developed a novel method called the Membrane Protein Crosslink Immuno-Precipitation, which enable identification of protein-protein interactions in the nuclear envelope in live cells. We identified several novel interactions of the inner nuclear membrane protein, Samp1, and studied the interaction between the Samp1 and the nuclear GTPase, Ran in detail. Samp1 can bind to Ran and is thus the first known transmembrane Ran binding protein and Samp1 might provide a local binding site for Ran in the inner nuclear membrane. We found that Samp1 also binds to the inner nuclear membrane protein, Emerin and Ran can regulate the Samp1-Emerin interaction in the nuclear envelope. During mitosis, Samp1 distributes in the mitotic spindle. Therefore, we investigated a possible functional role of Samp1 in the mitotic machinery. Samp1 depletion resulted in aneuploid phenotypes, metaphase prolongation and decreased distribution of γ-tubulin and β-tubulin in the mitotic spindle. We found that Samp1 can bind to γ-tubulin, which is essential for the microtubule nucleation and hence for the spindle stability. The new interesting features of Samp1 provide insights on the unforeseen functions of the nuclear envelope proteins.

Place, publisher, year, edition, pages
Stockholm: Department of Neurochemistry, Stockholm University, 2017
Keyword
Nuclear envelope, Samp1, Emerin, Ran and transmembrane proteins
National Category
Other Chemistry Topics
Research subject
Neurochemistry with Molecular Neurobiology
Identifiers
urn:nbn:se:su:diva-148432 (URN)978-91-7797-029-3 (ISBN)978-91-7797-030-9 (ISBN)
Public defence
2017-12-08, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 16 B, Stockholm, 10:00 (English)
Opponent
Supervisors
Note

At the time of the doctoral defense, the following papers were unpublished and had a status as follows: Paper 3: Manuscript. Paper 4: Manuscript.

Available from: 2017-11-15 Created: 2017-10-24 Last updated: 2017-11-16Bibliographically approved

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Vijayaraghavan, BalajeBergqvist, CecilaHallberg, Einar
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