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The nucleoplasmically exposed N-terminal domain of the inner nuclear membrane protein, Samp1, directly binds to the small monomeric GTPase, Ran
Stockholm University, Faculty of Science, Department of Neurochemistry.ORCID iD: 0000-0002-3481-1106
Stockholm University, Faculty of Science, Department of Neurochemistry.ORCID iD: 0000-0003-1287-0495
Stockholm University, Faculty of Science, Department of Neurochemistry.ORCID iD: 0000-0003-1476-6675
Stockholm University, Faculty of Science, Department of Neurochemistry.ORCID iD: 0000-0003-2092-457X
(English)Manuscript (preprint) (Other academic)
Keyword [en]
Samp1, Ran, protein-ptotein interaction, Nuclear envelope
National Category
Cell and Molecular Biology
Research subject
Neurochemistry and Neurotoxicology
Identifiers
URN: urn:nbn:se:su:diva-121617OAI: oai:DiVA.org:su-121617DiVA: diva2:860299
Funder
Swedish Cancer SocietySwedish Research Council
Available from: 2015-10-12 Created: 2015-10-12 Last updated: 2016-01-29Bibliographically approved
In thesis
1. Identification and characterization of nuclear envelope protein interactions
Open this publication in new window or tab >>Identification and characterization of nuclear envelope protein interactions
2015 (English)Licentiate thesis, comprehensive summary (Other academic)
Abstract [en]

The Nuclear envelope which surrounds the chromatin of eukaryotic cells contains more than a hundred transmembrane proteins. Mutations in some genes encoding nuclear envelope proteins give rise to human diseases including neurological disorders. The function of many nuclear envelope proteins is not well established. This is partly because nuclear envelope proteins and their interactions are difficult to study due to the inherent resistance to extraction of nuclear envelope proteins. We have developed a novel method called MCLIP, to identify interacting partners of nuclear envelope proteins in live cells. Using MCLIP, we found three new binding partners of the inner nuclear membrane protein Samp1: the intermediate filament protein Lamin B1, the LINC complex protein Sun1 and the G-protein Ran. Furthermore, using in vitro studies, we show that Samp1 binds both Emerin and Ran directly. We have also studied the interaction between Samp1 and Ran in detail.

Place, publisher, year, edition, pages
Stockholm: Department of Neurochemistry, Stockholm University, 2015. 48 p.
Keyword
Samp1, MCLIP, Nuclear envelope, Ran, Emerin
National Category
Chemical Sciences Biological Sciences Cell and Molecular Biology
Research subject
Neurochemistry with Molecular Neurobiology
Identifiers
urn:nbn:se:su:diva-122052 (URN)978-91-7649-289-5 (ISBN)
Presentation
2015-11-04, Heilbronnsalen, C458, Svante Arrhenius väg 16 B, Stockholm, 13:00 (English)
Opponent
Supervisors
Funder
Swedish Research Council, 621-2010-448Swedish Cancer Society, 110590Stiftelsen Olle Engkvist Byggmästare
Available from: 2015-10-23 Created: 2015-10-21 Last updated: 2015-10-23Bibliographically approved

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