Next Article in Journal
Regulation of the Adaptive Immune Response by the IκB Family Protein Bcl-3
Next Article in Special Issue
A Heterozygous ZMPSTE24 Mutation Associated with Severe Metabolic Syndrome, Ectopic Fat Accumulation, and Dilated Cardiomyopathy
Previous Article in Journal
The Regulation of NF-κB Subunits by Phosphorylation
Previous Article in Special Issue
Matefin/SUN-1 Phosphorylation on Serine 43 Is Mediated by CDK-1 and Required for Its Localization to Centrosomes and Normal Mitosis in C. elegans Embryos
Article Menu

Export Article

Open AccessArticle
Cells 2016, 5(1), 13; doi:10.3390/cells5010013

Src1 is a Protein of the Inner Nuclear Membrane Interacting with the Dictyostelium Lamin NE81

1
Institut für Biochemie und Biology, Department of Cell Biology, Universität Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Potsdam, Germany
2
Department of Biology, Clark University, 15 Maywood St., Worcester, MA 01610-1477, USA
3
Institut für Biochemie und Biology, Department of Animal Physiology, Universität Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Potsdam, Germany
*
Author to whom correspondence should be addressed.
Academic Editor: Thomas Dechat
Received: 29 January 2016 / Revised: 9 March 2016 / Accepted: 11 March 2016 / Published: 18 March 2016
(This article belongs to the Collection Lamins and Laminopathies)
View Full-Text   |   Download PDF [5038 KB, uploaded 18 March 2016]   |  

Abstract

The nuclear envelope (NE) consists of the outer and inner nuclear membrane (INM), whereby the latter is bound to the nuclear lamina. Src1 is a Dictyostelium homologue of the helix-extension-helix family of proteins, which also includes the human lamin-binding protein MAN1. Both endogenous Src1 and GFP-Src1 are localized to the NE during the entire cell cycle. Immuno-electron microscopy and light microscopy after differential detergent treatment indicated that Src1 resides in the INM. FRAP experiments with GFP-Src1 cells suggested that at least a fraction of the protein could be stably engaged in forming the nuclear lamina together with the Dictyostelium lamin NE81. Both a BioID proximity assay and mis-localization of soluble, truncated mRFP-Src1 at cytosolic clusters consisting of an intentionally mis-localized mutant of GFP-NE81 confirmed an interaction of Src1 and NE81. Expression GFP-Src11–646, a fragment C-terminally truncated after the first transmembrane domain, disrupted interaction of nuclear membranes with the nuclear lamina, as cells formed protrusions of the NE that were dependent on cytoskeletal pulling forces. Protrusions were dependent on intact microtubules but not actin filaments. Our results indicate that Src1 is required for integrity of the NE and highlight Dictyostelium as a promising model for the evolution of nuclear architecture. View Full-Text
Keywords: Dictyostelium; lamin; nuclear lamina; nucleus; nucleolus; HeH-protein; LEM-domain protein Dictyostelium; lamin; nuclear lamina; nucleus; nucleolus; HeH-protein; LEM-domain protein
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Batsios, P.; Ren, X.; Baumann, O.; Larochelle, D.A.; Gräf, R. Src1 is a Protein of the Inner Nuclear Membrane Interacting with the Dictyostelium Lamin NE81. Cells 2016, 5, 13.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Cells EISSN 2073-4409 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top