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High mobility of proteins in the mammalian cell nucleus

Author

Listed:
  • Robert D. Phair

    (BioInformatics Services)

  • Tom Misteli

    (National Cancer Institute, NIH)

Abstract

The mammalian cell nucleus contains numerous sub-compartments, which have been implicated in essential processes such as transcription and splicing1,2. The mechanisms by which nuclear compartments are formed and maintained are unclear. More fundamentally, it is not known how proteins move within the cell nucleus. We have measured the kinetic properties of proteins in the nucleus of living cells using photobleaching techniques. Here we show that proteins involved in diverse nuclear processes move rapidly throughout the entire nucleus. Protein movement is independent of energy, which indicates that proteins may use a passive mechanism of movement. Proteins rapidly associate and dissociate with nuclear compartments. Using kinetic modelling, we determined residence times and steady-state fluxes of molecules in two main nuclear compartments. These data show that many nuclear proteins roam the cell nucleus in vivo and that nuclear compartments are the reflection of the steady-state association/dissociation of its ‘residents’ with the nucleoplasmic space. Our observations have conceptual implications for understanding nuclear architecture and how nuclear processes are organized in vivo.

Suggested Citation

  • Robert D. Phair & Tom Misteli, 2000. "High mobility of proteins in the mammalian cell nucleus," Nature, Nature, vol. 404(6778), pages 604-609, April.
    • Handle: RePEc:nat:nature:v:404:y:2000:i:6778:d:10.1038_35007077
    DOI: 10.1038/35007077
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    Cited by:

    1. Huanqing Cui & Yage Zhang & Sihan Liu & Yang Cao & Qingming Ma & Yuan Liu & Haisong Lin & Chang Li & Yang Xiao & Sammer Ul Hassan & Ho Cheung Shum, 2024. "Thermo-responsive aqueous two-phase system for two-level compartmentalization," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    2. Yifeng Qi & Bin Zhang, 2021. "Chromatin network retards nucleoli coalescence," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
    3. Lisa Streit & Timo Kuhn & Thomas Vomhof & Verena Bopp & Albert C. Ludolph & Jochen H. Weishaupt & J. Christof M. Gebhardt & Jens Michaelis & Karin M. Danzer, 2022. "Stress induced TDP-43 mobility loss independent of stress granules," Nature Communications, Nature, vol. 13(1), pages 1-18, December.
    4. Gillie Benchorin & Richard Jangwon Cho & Maggie Jiaqi Li & Natalia Molotkova & Minoree Kohwi, 2024. "Dan forms condensates in neuroblasts and regulates nuclear architecture and progenitor competence in vivo," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    5. Marta Vicioso-Mantis & Raquel Fueyo & Claudia Navarro & Sara Cruz-Molina & Wilfred F. J. Ijcken & Elena Rebollo & Álvaro Rada-Iglesias & Marian A. Martínez-Balbás, 2022. "JMJD3 intrinsically disordered region links the 3D-genome structure to TGFβ-dependent transcription activation," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    6. Brooke E. Danielsson & Bobin George Abraham & Elina Mäntylä & Jolene I. Cabe & Carl R. Mayer & Anna Rekonen & Frans Ek & Daniel E. Conway & Teemu O. Ihalainen, 2023. "Nuclear lamina strain states revealed by intermolecular force biosensor," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    7. Guo Sheng Han & Zu Guo Yu & Vo Anh & Anaththa P D Krishnajith & Yu-Chu Tian, 2013. "An Ensemble Method for Predicting Subnuclear Localizations from Primary Protein Structures," PLOS ONE, Public Library of Science, vol. 8(2), pages 1-14, February.

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