Nesprin-2 Interacts with Condensin Component SMC2
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 do...
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| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2017-01-01
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| Series: | International Journal of Cell Biology |
| Online Access: | http://dx.doi.org/10.1155/2017/8607532 |
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| author | Xin Xing Carmen Mroß Linlin Hao Martina Munck Alexandra Herzog Clara Mohr C. P. Unnikannan Pranav Kelkar Angelika A. Noegel Ludwig Eichinger Sascha Neumann |
| author_facet | Xin Xing Carmen Mroß Linlin Hao Martina Munck Alexandra Herzog Clara Mohr C. P. Unnikannan Pranav Kelkar Angelika A. Noegel Ludwig Eichinger Sascha Neumann |
| author_sort | Xin Xing |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-9b4d03bfa44347f8a417f515a99fdde0 |
| institution | Kabale University |
| issn | 1687-8876 1687-8884 |
| language | English |
| publishDate | 2017-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | International Journal of Cell Biology |
| spelling | doaj-art-9b4d03bfa44347f8a417f515a99fdde02025-02-03T01:25:34ZengWileyInternational Journal of Cell Biology1687-88761687-88842017-01-01201710.1155/2017/86075328607532Nesprin-2 Interacts with Condensin Component SMC2Xin Xing0Carmen Mroß1Linlin Hao2Martina Munck3Alexandra Herzog4Clara Mohr5C. P. Unnikannan6Pranav Kelkar7Angelika A. Noegel8Ludwig Eichinger9Sascha Neumann10Institute of Biochemistry I, Medical Faculty, University Hospital Cologne, Joseph-Stelzmann-Str. 52, 50931 Cologne, GermanyInstitute of Biochemistry I, Medical Faculty, University Hospital Cologne, Joseph-Stelzmann-Str. 52, 50931 Cologne, GermanyInstitute of Biochemistry I, Medical Faculty, University Hospital Cologne, Joseph-Stelzmann-Str. 52, 50931 Cologne, GermanyInstitute of Biochemistry I, Medical Faculty, University Hospital Cologne, Joseph-Stelzmann-Str. 52, 50931 Cologne, GermanyInstitute of Biochemistry I, Medical Faculty, University Hospital Cologne, Joseph-Stelzmann-Str. 52, 50931 Cologne, GermanyInstitute of Biochemistry I, Medical Faculty, University Hospital Cologne, Joseph-Stelzmann-Str. 52, 50931 Cologne, GermanyInstitute of Biochemistry I, Medical Faculty, University Hospital Cologne, Joseph-Stelzmann-Str. 52, 50931 Cologne, GermanyInstitute of Biochemistry I, Medical Faculty, University Hospital Cologne, Joseph-Stelzmann-Str. 52, 50931 Cologne, GermanyInstitute of Biochemistry I, Medical Faculty, University Hospital Cologne, Joseph-Stelzmann-Str. 52, 50931 Cologne, GermanyInstitute of Biochemistry I, Medical Faculty, University Hospital Cologne, Joseph-Stelzmann-Str. 52, 50931 Cologne, GermanyInstitute of Biochemistry I, Medical Faculty, University Hospital Cologne, Joseph-Stelzmann-Str. 52, 50931 Cologne, GermanyThe 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.http://dx.doi.org/10.1155/2017/8607532 |
| spellingShingle | Xin Xing Carmen Mroß Linlin Hao Martina Munck Alexandra Herzog Clara Mohr C. P. Unnikannan Pranav Kelkar Angelika A. Noegel Ludwig Eichinger Sascha Neumann Nesprin-2 Interacts with Condensin Component SMC2 International Journal of Cell Biology |
| title | Nesprin-2 Interacts with Condensin Component SMC2 |
| title_full | Nesprin-2 Interacts with Condensin Component SMC2 |
| title_fullStr | Nesprin-2 Interacts with Condensin Component SMC2 |
| title_full_unstemmed | Nesprin-2 Interacts with Condensin Component SMC2 |
| title_short | Nesprin-2 Interacts with Condensin Component SMC2 |
| title_sort | nesprin 2 interacts with condensin component smc2 |
| url | http://dx.doi.org/10.1155/2017/8607532 |
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