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International Journal of Cell Biology
Volume 2017, Article ID 8607532, 15 pages
Research Article

Nesprin-2 Interacts with Condensin Component SMC2

1Institute of Biochemistry I, Medical Faculty, University Hospital Cologne, Joseph-Stelzmann-Str. 52, 50931 Cologne, Germany
2Center for Molecular Medicine Cologne (CMMC) and Cologne Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), Medical Faculty, University of Cologne, Cologne, Germany

Correspondence should be addressed to Angelika A. Noegel; ed.nleok-inu@legeon and Ludwig Eichinger; ed.nleok-inu@regnihcie.giwdul

Received 27 July 2017; Revised 17 November 2017; Accepted 7 December 2017; Published 27 December 2017

Academic Editor: Arnoud Sonnenberg

Copyright © 2017 Xin Xing et al. 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.


The nuclear envelope proteins, Nesprins, have been primarily studied during interphase where they function in maintaining nuclear shape, size, and positioning. We analyze here the function of Nesprin-2 in chromatin interactions in interphase and dividing cells. We characterize a region in the rod domain of Nesprin-2 that is predicted as SMC domain (aa 1436–1766). We show that this domain can interact with itself. It furthermore has the capacity to bind to SMC2 and SMC4, the core subunits of condensin. The interaction was observed during all phases of the cell cycle; it was particularly strong during S phase and persisted also during mitosis. Nesprin-2 knockdown did not affect condensin distribution; however we noticed significantly higher numbers of chromatin bridges in Nesprin-2 knockdown cells in anaphase. Thus, Nesprin-2 may have an impact on chromosomes which might be due to its interaction with condensins or to indirect mechanisms provided by its interactions at the nuclear envelope.