Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
The integral nuclear membrane protein, Samp1 modulates importin-β and NuMA in the mitotic spindle
Stockholm University, Faculty of Science, Department of Neurochemistry.
Stockholm University, Faculty of Science, Department of Neurochemistry.ORCID iD: 0000-0003-1476-6675
Stockholm University, Faculty of Science, Department of Neurochemistry.ORCID iD: 0000-0003-1287-0495
Stockholm University, Faculty of Science, Department of Neurochemistry.
Show others and affiliations
(English)Manuscript (preprint) (Other academic)
Keywords [en]
Samp1, mitotic spindle, centrosome, LINC complex, Lamina, Sun1, mitosis
National Category
Biological Sciences Chemical Sciences
Research subject
Neurochemistry with Molecular Neurobiology
Identifiers
URN: urn:nbn:se:su:diva-109192OAI: oai:DiVA.org:su-109192DiVA, id: diva2:763444
Funder
Swedish Research Council, 621-2010-448Swedish Cancer Society, 110590Available from: 2014-11-14 Created: 2014-11-14 Last updated: 2016-01-29Bibliographically approved
In thesis
1. Nuclear envelope protein interaction studies
Open this publication in new window or tab >>Nuclear envelope protein interaction studies
2014 (English)Licentiate thesis, comprehensive summary (Other academic)
Abstract [en]

The nuclear envelope (NE) separating the nucleoplasm from cytoplasm consists of two concentric lipid membranes, the outer (ONM) and inner (INM) nuclear membranes, the nuclear pore complexes (NPCs) and an underlying nuclear lamina network. The INM contains more than 100 unique transmembrane proteins of which only a few have been characterized. This thesis is focused on one of these INM proteins, Samp1 (Spindle associated membrane protein 1)

Protein-protein interactions in the NE have been difficult to study due to the resistance of NE proteins to extraction. We have established a reversible in vivo crosslinking immunoprecipitation method called, MCLIP (Membrane protein Cross-Link ImmunoPrecipitation) to overcome this problem. Using MCLIP we were able to show that, Samp1 specifically interacts with Emerin, Lamin B1, Sun1 and the small GTPase Ran. We also showed that, the nucleoplasmic domain of Samp1 and Emerin can interact with each other directly.

Furthermore, we investigated the functional role of Samp1 in mitosis. Samp1 depletion gave rise to aneuploid phenotypes and signs of destabilization of the mitotic spindle. Using MCLIP, in mitotic cells, we showed that, Samp1 interacts with Ran and Importin-β, two key players of mitotic spindle assembly. We observed that, Samp1 modulates the level of Importin-β and NuMA in the mitotic spindle, which may explain the mitotic defects and aberrant phenotypes observed in Samp1 depleted cells. These findings show that Samp1 plays an important role in spindle stabilization and chromosome segregation. 

Place, publisher, year, edition, pages
Stockholm: Department of Neurochemistry, Stockholm University, 2014
Keywords
Samp1, Nuclear envelope, protein interactions, chemical crosslinking, proteomics
National Category
Biochemistry and Molecular Biology
Research subject
Neurochemistry with Molecular Neurobiology
Identifiers
urn:nbn:se:su:diva-109194 (URN)978-91-7649-041-9 (ISBN)
Presentation
2014-12-16, Heilbronnsalen, Svante Arrhenius väg 16 B, Stockholm, 12:15 (English)
Opponent
Supervisors
Available from: 2014-11-21 Created: 2014-11-14 Last updated: 2015-03-17Bibliographically approved

Open Access in DiVA

No full text in DiVA

Search in DiVA

By author/editor
Larsson, Veronica J.Figueroa, Ricardo A.Jafferali, Mohammed HakimMarkus, RobertHallberg, Einar
By organisation
Department of Neurochemistry
Biological SciencesChemical Sciences

Search outside of DiVA

GoogleGoogle Scholar

urn-nbn

Altmetric score

urn-nbn
Total: 92 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf