Droplet organelles?
Cells contain numerous, molecularly distinct cellular compartments that are not enclosed by lipid bilayers. These compartments are implicated in a wide range of cellular activities, and they have been variously described as bodies, granules, or organelles. Recent evidence suggests that a liquid–liqu...
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| Published in | The EMBO journal Vol. 35; no. 15; pp. 1603 - 1612 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Blackwell Publishing Ltd
01.08.2016
Nature Publishing Group UK Springer Nature B.V John Wiley and Sons Inc |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Cells contain numerous, molecularly distinct cellular compartments that are not enclosed by lipid bilayers. These compartments are implicated in a wide range of cellular activities, and they have been variously described as bodies, granules, or organelles. Recent evidence suggests that a liquid–liquid phase separation (LLPS) process may drive their formation, possibly justifying the unifying term “droplet organelle”. A veritable deluge of recent publications points to the importance of low‐complexity proteins and RNA in determining the physical properties of phase‐separated structures. Many of the proteins linked to such structures are implicated in human diseases, such as amyotrophic lateral sclerosis (ALS). We provide an overview of the organizational principles that characterize putative “droplet organelles” in healthy and diseased cells, connecting protein biochemistry with cell physiology.
Graphical Abstract
Non‐membrane‐bound cellular structures such as nucleoli, stress granules, Cajal and P bodies have been long established. Recent data reviewed by Neugebauer and colleagues delineate liquid–liquid phase separation processes that underlie the dynamic nature of these organelles composed of low‐complexity proteins and RNA. |
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| AbstractList | Cells contain numerous, molecularly distinct cellular compartments that are not enclosed by lipid bilayers. These compartments are implicated in a wide range of cellular activities, and they have been variously described as bodies, granules, or organelles. Recent evidence suggests that a liquid–liquid phase separation (
LLPS
) process may drive their formation, possibly justifying the unifying term “droplet organelle”. A veritable deluge of recent publications points to the importance of low‐complexity proteins and
RNA
in determining the physical properties of phase‐separated structures. Many of the proteins linked to such structures are implicated in human diseases, such as amyotrophic lateral sclerosis (
ALS
). We provide an overview of the organizational principles that characterize putative “droplet organelles” in healthy and diseased cells, connecting protein biochemistry with cell physiology. Cells contain numerous, molecularly distinct cellular compartments that are not enclosed by lipid bilayers. These compartments are implicated in a wide range of cellular activities, and they have been variously described as bodies, granules, or organelles. Recent evidence suggests that a liquid-liquid phase separation (LLPS) process may drive their formation, possibly justifying the unifying term "droplet organelle". A veritable deluge of recent publications points to the importance of low-complexity proteins and RNA in determining the physical properties of phase-separated structures. Many of the proteins linked to such structures are implicated in human diseases, such as amyotrophic lateral sclerosis (ALS). We provide an overview of the organizational principles that characterize putative "droplet organelles" in healthy and diseased cells, connecting protein biochemistry with cell physiology.Cells contain numerous, molecularly distinct cellular compartments that are not enclosed by lipid bilayers. These compartments are implicated in a wide range of cellular activities, and they have been variously described as bodies, granules, or organelles. Recent evidence suggests that a liquid-liquid phase separation (LLPS) process may drive their formation, possibly justifying the unifying term "droplet organelle". A veritable deluge of recent publications points to the importance of low-complexity proteins and RNA in determining the physical properties of phase-separated structures. Many of the proteins linked to such structures are implicated in human diseases, such as amyotrophic lateral sclerosis (ALS). We provide an overview of the organizational principles that characterize putative "droplet organelles" in healthy and diseased cells, connecting protein biochemistry with cell physiology. Cells contain numerous, molecularly distinct cellular compartments that are not enclosed by lipid bilayers. These compartments are implicated in a wide range of cellular activities, and they have been variously described as bodies, granules, or organelles. Recent evidence suggests that a liquid–liquid phase separation (LLPS) process may drive their formation, possibly justifying the unifying term “droplet organelle”. A veritable deluge of recent publications points to the importance of low‐complexity proteins and RNA in determining the physical properties of phase‐separated structures. Many of the proteins linked to such structures are implicated in human diseases, such as amyotrophic lateral sclerosis (ALS). We provide an overview of the organizational principles that characterize putative “droplet organelles” in healthy and diseased cells, connecting protein biochemistry with cell physiology. Graphical Abstract Non‐membrane‐bound cellular structures such as nucleoli, stress granules, Cajal and P bodies have been long established. Recent data reviewed by Neugebauer and colleagues delineate liquid–liquid phase separation processes that underlie the dynamic nature of these organelles composed of low‐complexity proteins and RNA. Cells contain numerous, molecularly distinct cellular compartments that are not enclosed by lipid bilayers. These compartments are implicated in a wide range of cellular activities, and they have been variously described as bodies, granules, or organelles. Recent evidence suggests that a liquid–liquid phase separation (LLPS) process may drive their formation, possibly justifying the unifying term “droplet organelle”. A veritable deluge of recent publications points to the importance of low‐complexity proteins and RNA in determining the physical properties of phase‐separated structures. Many of the proteins linked to such structures are implicated in human diseases, such as amyotrophic lateral sclerosis (ALS). We provide an overview of the organizational principles that characterize putative “droplet organelles” in healthy and diseased cells, connecting protein biochemistry with cell physiology. Non‐membrane‐bound cellular structures such as nucleoli, stress granules, Cajal and P bodies have been long established. Recent data reviewed by Neugebauer and colleagues delineate liquid–liquid phase separation processes that underlie the dynamic nature of these organelles composed of low‐complexity proteins and RNA. Cells contain numerous, molecularly distinct cellular compartments that are not enclosed by lipid bilayers. These compartments are implicated in a wide range of cellular activities, and they have been variously described as bodies, granules, or organelles. Recent evidence suggests that a liquid-liquid phase separation (LLPS) process may drive their formation, possibly justifying the unifying term "droplet organelle". A veritable deluge of recent publications points to the importance of low-complexity proteins and RNA in determining the physical properties of phase-separated structures. Many of the proteins linked to such structures are implicated in human diseases, such as amyotrophic lateral sclerosis (ALS). We provide an overview of the organizational principles that characterize putative "droplet organelles" in healthy and diseased cells, connecting protein biochemistry with cell physiology. |
| Author | Courchaine, Edward M Neugebauer, Karla M Lu, Alice |
| AuthorAffiliation | 1 Department of Molecular Biophysics and Biochemistry Yale University New Haven CT USA |
| AuthorAffiliation_xml | – name: 1 Department of Molecular Biophysics and Biochemistry Yale University New Haven CT USA |
| Author_xml | – sequence: 1 givenname: Edward M surname: Courchaine fullname: Courchaine, Edward M organization: Department of Molecular Biophysics and Biochemistry, Yale University, CT, New Haven, USA – sequence: 2 givenname: Alice surname: Lu fullname: Lu, Alice organization: Department of Molecular Biophysics and Biochemistry, Yale University, CT, New Haven, USA – sequence: 3 givenname: Karla M surname: Neugebauer fullname: Neugebauer, Karla M email: karla.neugebauer@yale.edu organization: Department of Molecular Biophysics and Biochemistry, Yale University, CT, New Haven, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/27357569$$D View this record in MEDLINE/PubMed |
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| Keywords | Liquid‐liquid phase separation RNP granules nuclear bodies low‐complexity domain |
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| SubjectTerms | Amyotrophic lateral sclerosis Biochemistry Cell Physiological Phenomena Cellular biology Cytosol - chemistry EMBO20 EMBO27 EMBO36 Liquid-liquid phase separation low-complexity domain Macromolecular Substances - metabolism Molecular biology Multienzyme Complexes - metabolism nuclear bodies Physical properties Proteins Review RNP granules |
| Title | Droplet organelles? |
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