The liquid nucleome - phase transitions in the nucleus at a glance

doi:10.1242/jcs.235093

Review

. 2019 Nov 21;132(22):jcs235093.

doi: 10.1242/jcs.235093.

The liquid nucleome - phase transitions in the nucleus at a glance

Amy R Strom¹, Clifford P Brangwynne²

Affiliations

¹ Department of Chemical and Biological Engineering, Howard Hughes Medical Institute, Princeton University, Princeton NJ 08544, USA.
² Department of Chemical and Biological Engineering, Howard Hughes Medical Institute, Princeton University, Princeton NJ 08544, USA cbrangwy@princeton.edu.

PMID: 31754043
PMCID: PMC6899023
DOI: 10.1242/jcs.235093

Review

The liquid nucleome - phase transitions in the nucleus at a glance

Amy R Strom et al. J Cell Sci. 2019.

. 2019 Nov 21;132(22):jcs235093.

doi: 10.1242/jcs.235093.

Authors

Amy R Strom¹, Clifford P Brangwynne²

Affiliations

¹ Department of Chemical and Biological Engineering, Howard Hughes Medical Institute, Princeton University, Princeton NJ 08544, USA.
² Department of Chemical and Biological Engineering, Howard Hughes Medical Institute, Princeton University, Princeton NJ 08544, USA cbrangwy@princeton.edu.

PMID: 31754043
PMCID: PMC6899023
DOI: 10.1242/jcs.235093

Abstract

Cells organize membrane-less internal compartments through a process called liquid-liquid phase separation (LLPS) to create chemically distinct compartments, referred to as condensates, which emerge from interactions among biological macromolecules. These condensates include various cytoplasmic structures such as P-granules and stress granules. However, an even wider array of condensates subcompartmentalize the cell nucleus, forming liquid-like structures that range from nucleoli and Cajal bodies to nuclear speckles and gems. Phase separation provides a biophysical assembly mechanism underlying this non-covalent form of fluid compartmentalization and functionalization. In this Cell Science at a Glance article and the accompanying poster, we term these phase-separated liquids that organize the nucleus the liquid nucleome; we discuss examples of biological phase transitions in the nucleus, how the cell utilizes biophysical aspects of phase separation to form and regulate condensates, and suggest interpretations for the role of phase separation in nuclear organization and function.

Keywords: Chromatin; Nuclear organization; Nucleolus; Phase separation.

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Conflict of interest statement

Competing interestsThe authors declare no competing or financial interests.

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References

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[1] Aasland R. and Stewart A. F. (1995). The chromo shadow domain, a second chromo domain in heterochromatin-binding protein 1, HP1. Nucleic Acids Res. 23, 3168-3173. 10.1093/nar/23.16.3168 - DOI - PMC - PubMed

[2] Aasland R. and Stewart A. F. (1995). The chromo shadow domain, a second chromo domain in heterochromatin-binding protein 1, HP1. Nucleic Acids Res. 23, 3168-3173. 10.1093/nar/23.16.3168 - DOI - PMC - PubMed

[3] Almouzni G. and Probst A. V. (2011). Heterochromatin maintenance and establishment: lessons from the mouse pericentromere. Nucleus 2, 332-338. 10.4161/nucl.2.5.17707 - DOI - PubMed

[4] Almouzni G. and Probst A. V. (2011). Heterochromatin maintenance and establishment: lessons from the mouse pericentromere. Nucleus 2, 332-338. 10.4161/nucl.2.5.17707 - DOI - PubMed

[5] Altmeyer M., Neelsen K. J., Teloni F., Pozdnyakova I., Pellegrino S., Grøfte M., Rask M.-B. D., Streicher W., Jungmichel S., Nielsen M. L. et al. (2015). Liquid demixing of intrinsically disordered proteins is seeded by poly(ADP-ribose). Nat. Commun. 6, 8088 10.1038/ncomms9088 - DOI - PMC - PubMed

[6] Altmeyer M., Neelsen K. J., Teloni F., Pozdnyakova I., Pellegrino S., Grøfte M., Rask M.-B. D., Streicher W., Jungmichel S., Nielsen M. L. et al. (2015). Liquid demixing of intrinsically disordered proteins is seeded by poly(ADP-ribose). Nat. Commun. 6, 8088 10.1038/ncomms9088 - DOI - PMC - PubMed

[7] Aonbangkhen C., Zhang H., Wu D. Z., Lampson M. A. and Chenoweth D. M. (2018). Reversible control of protein localization in living cells using a photocaged-photocleavable chemical dimerizer. J. Am. Chem. Soc. 140, 11926-11930. 10.1021/jacs.8b07753 - DOI - PMC - PubMed

[8] Aonbangkhen C., Zhang H., Wu D. Z., Lampson M. A. and Chenoweth D. M. (2018). Reversible control of protein localization in living cells using a photocaged-photocleavable chemical dimerizer. J. Am. Chem. Soc. 140, 11926-11930. 10.1021/jacs.8b07753 - DOI - PMC - PubMed

[9] Banani S. F., Lee H. O., Hyman A. A. and Rosen M. K. (2017). Biomolecular condensates: organizers of cellular biochemistry. Nat. Rev. Mol. Cell Biol. 18, 285-298. 10.1038/nrm.2017.7 - DOI - PMC - PubMed

[10] Banani S. F., Lee H. O., Hyman A. A. and Rosen M. K. (2017). Biomolecular condensates: organizers of cellular biochemistry. Nat. Rev. Mol. Cell Biol. 18, 285-298. 10.1038/nrm.2017.7 - DOI - PMC - PubMed

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The liquid nucleome - phase transitions in the nucleus at a glance

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The liquid nucleome - phase transitions in the nucleus at a glance

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Affiliations

Abstract

Conflict of interest statement

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