The tail domain of lamin B1 is more strongly modulated by divalent cations than lamin A.

@article{Ganesh2015TheTD,
  title={The tail domain of lamin B1 is more strongly modulated by divalent cations than lamin A.},
  author={Sairaam Ganesh and Zhao Qin Qin and Stephen T. Spagnol and Matthew T. Biegler and Kelli A Coffey and Agnieszka Kalinowski and Markus J Buehler and Kris Noel Dahl},
  journal={Nucleus},
  year={2015},
  volume={6 3},
  pages={203-11}
}
The nucleoskeleton contains mainly nuclear intermediate filaments made of lamin proteins. Lamins provide nuclear structure and also play a role in various nuclear processes including signal transduction, transcription regulation and chromatin organization. The disparate functions of lamins may be related to the intrinsic disorder of the tail domains, which allows for altered and promiscuous binding. Here, we show modulation of lamin tail domain structures in the presence of divalent cations. We… CONTINUE READING
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