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Phase separation in biology; functional organization of a higher order

Mitrea, Diana M., Kriwacki, Richard W.·2016·Cell Communication and Signaling
DOI 10.1186/s12964-015-0125-7PMC PMC4700675
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Fig. 1 Macromolecular condensation mediates the formation of membrane-less organelles. Membrane-less organelles are dynamic structures formed via a polymer-condensation-like, concentration-dependent phase separation mechanism. The critical concentration threshold (grey line) for phase separation can be tuned within a range of concentrations (shaded green box) through physico-chemical alterations to the system (i.e., posttranslational modifications to domains and/or motifs that alter the affinity of their interactions, changes in temperature, altered ionic strength, etc.). These changes can drive phase separation and assembly of membrane-less organelles, or their disassembly
Fig. 1 Macromolecular condensation mediates the formation of membrane-less organelles. Membrane-less organelles are dynamic structures formed via a polymer-condensation-like, concentration-dependent phase separation mechanism. The critical concentration threshold (grey line) for phase separation can be tuned within a range of concentrations (shaded green box) through physico-chemical alterations to the system (i.e., posttranslational modifications to domains and/or motifs that alter the affinity of their interactions, changes in temperature, altered ionic strength, etc.). These changes can drive phase separation and assembly of membrane-less organelles, or their disassemblyCC BY · PubMed Central
Fig. 2 Molecular basis for membrane-less organelles assembly. The proteins enriched within the matrices of membrane-less organelles commonly exhibit multiple modules that create multivalency, including folded binding domains (red) and low complexity regions (purple). Valency is often amplified by domains that enable homo-, or hetero-oligomerization (orange). Interactions between proteins containing different combinations of these interaction modules provide a framework for building a heterogeneous, infinitely expandable network within membrane-less organelles. Formation of this type of network drives phase separation when the critical concentration threshold is reached. For many of the examples discussed herein, active RNA transcription is needed for membrane-less organelle assembly. We hypothesize that expression of RNA in excess of a critical concentration threshold is needed to nucleate interactions with specific, multi-modular proteins, and for nucleating formation of membrane-less organelles. Stress signals can alter the multivalent interactions that drive phase separation and lead to partial or complete disassembly of the organelle
Fig. 2 Molecular basis for membrane-less organelles assembly. The proteins enriched within the matrices of membrane-less organelles commonly exhibit multiple modules that create multivalency, including folded binding domains (red) and low complexity regions (purple). Valency is often amplified by domains that enable homo-, or hetero-oligomerization (orange). Interactions between proteins containing different combinations of these interaction modules provide a framework for building a heterogeneous, infinitely expandable network within membrane-less organelles. Formation of this type of network drives phase separation when the critical concentration threshold is reached. For many of the examples discussed herein, active RNA transcription is needed for membrane-less organelle assembly. We hypothesize that expression of RNA in excess of a critical concentration threshold is needed to nucleate interactions with specific, multi-modular proteins, and for nucleating formation of membrane-less organelles. Stress signals can alter the multivalent interactions that drive phase separation and lead to partial or complete disassembly of the organelleCC BY · PubMed Central

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Cited by

See all 726

Metadata

Authors
Mitrea, D. M., & Kriwacki, R. W.
Venue
Cell Communication and Signaling
Publisher
Springer Science and Business Media LLC
Published
2016-01-05
Volume
14
Issue
1
ISSN
1478-811X
DOI
10.1186/s12964-015-0125-7
PMC
PMC4700675
Cited by
726
References
3
Language
en
Licence
Funders
  • National Institutes of Health (1R01GM115634)
  • National Cancer Institute (P30CA21765)
  • ALSAC

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

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This page
CoChat. (2026). Citation check: Phase separation in biology; functional organization of a higher order. https://app.cochat.ai/papers/10.1186/s12964-015-0125-7
The paper
Mitrea, D. M., & Kriwacki, R. W. (2016). Phase separation in biology; functional organization of a higher order. Cell Communication and Signaling. https://doi.org/10.1186/s12964-015-0125-7

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.