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.
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Background Although pneumonia is a leading cause of death in New York City (NYC), limited data exist about the settings in which pneumonia ...
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Summary We tested whether prophylactic droperidol and ondansetron, in combination with a moderate dose of dexamethasone, were equally effe...
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by Demin Li, Carol Bentley, Jenna Yates, Maryam Salimi, Jenny Greig, Sarah Wiblin, Tasneem Hassanali, Alison H. Banham Therapeutic monoclon...
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ACS Nano DOI: 10.1021/acsnano.6b08567 from #AlexandrosSfakianakis via Alexandros G.Sfakianakis on Inoreader http://ift.tt/2oNpdhD via...
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Abstract Dermoscopy has demonstrated clinical benefits in improving early melanoma diagnosis and reducing unnecessary biopsies. Despite th...
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