The Eukaryotic CO2-Concentrating Organelle Is Liquid-like and Exhibits Dynamic Reorganization

Rosenzweig, Elizabeth S. Freeman; Xu, Bai; Cuellar, Luis Kuhn; Martínez-Sánchez, Antonio; Schaffer, Miroslava; Strauß, Michael; Cartwright, Heather; Ronceray, Pierre; Plitzko, Jürgen M.; Förster, Friedrich; Wingreen, Ned S.; Engel, Benjamin D.; Mackinder, Luke C. M.; Jonikas, Martin C.

doi:10.1016/j.cell.2017.08.008

Cited by 343 publications

(366 citation statements)

References 78 publications

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“…EPYC1 is highly disordered and likely forms weak interactions with Rubisco. Although both components were found to diffuse within the pyrenoid, they did so at different rates, suggesting that the diffusing unit is not a stable EPYC1–Rubisco complex …”

Section: Three Examples: Proteins Mlos and Functionmentioning

confidence: 96%

“…Magic number effects in the interaction stoichiometry of the EPYC1–Rubisco complex may lead to unique macroscopic effects. In computational models, eight binding sites of the Rubisco holoenzyme may be fully occupied by two EPYC1 proteins, each thought to contain four sites . This stoichiometry gives rise to a magic number effect in the simulations.…”

Section: Three Examples: Proteins Mlos and Functionmentioning

confidence: 99%

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Physical Chemistry of Cellular Liquid‐Phase Separation

Bentley

Frey

Deniz

2019

Chemistry A European J

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Compartmentalization of biochemical processes is essential for cell function. Although membrane‐bound organelles are well studied in this context, recent work has shown that phase separation is a key contributor to cellular compartmentalization through the formation of liquid‐like membraneless organelles (MLOs). In this Minireview, the key mechanistic concepts that underlie MLO dynamics and function are first briefly discussed, including the relevant noncovalent interaction chemistry and polymer physical chemistry. Next, a few examples of MLOs and relevant proteins are given, along with their functions, which highlight the relevance of the above concepts. The developing area of active matter and non‐equilibrium systems, which can give rise to unexpected effects in fluctuating cellular conditions, are also discussed. Finally, our thoughts for emerging and future directions in the field are discussed, including in vitro and in vivo studies of MLO physical chemistry and function.

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Section: Three Examples: Proteins Mlos and Functionmentioning

confidence: 96%

Section: Three Examples: Proteins Mlos and Functionmentioning

confidence: 99%

Physical Chemistry of Cellular Liquid‐Phase Separation

Bentley

Frey

Deniz

2019

Chemistry A European J

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“…Notably, pyrenoids are remarkably dynamic, fluctuating in size and composition – particularly their Rubisco content – in response to changes in CO 2 , light intensity, and developmental cues 34 . It appears that at least some of this versatility is afforded by the phase-separated nature of the pyrenoid 15 .…”

Section: Regulating Phase Separationmentioning

confidence: 99%

“…At the same time, the list of such membraneless ‘organelles’ is ever-growing: germ granules 8 , nucleoli 9 , nuclear speckles 10 , P-bodies 11 , stress granules 12 , paraspeckles 13 , the Balbiani body 14 , pyrenoids 15 , chaperone bodies 16 , dynein assembly particles 17 , heterochromatin 18 , and centrosomes 19,20 have all been characterized in this way. Although inclusion within a membrane has classically defined cellular compartments, the pervasiveness of protein phase separation suggests that it is also a fundamental organizing principle of cell biology.…”

Section: Introductionmentioning

confidence: 99%

It Pays To Be in Phase

2018

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To survive, organisms must orchestrate many competing biochemical and regulatory processes in time and space. Recent work has suggested that the underlying chemical properties of some biomolecules allow them to self-organize, and that life may have exploited this property to organize biochemistry in space and time within cells. Such phase separation is ubiquitous, particularly among the many regulatory proteins that harbor prion-like intrinsically disordered domains. And yet, despite evident regulation by post-translational modification and myriad other stimuli, the biological significance of many phase-separated compartments remains uncertain. Many potential functions have been proposed but far fewer have been demonstrated. A burgeoning subfield at the intersection of cell biology and polymer physics has defined the biophysical underpinnings that govern the genesis and stability of these particles. The picture is complex: many assemblies are composed of multiple proteins that each have the capacity to phase separate. Here, we briefly discuss this foundational work and survey recent efforts combining targeted biochemical perturbations and quantitative modeling to specifically address the diverse roles that phase separation processes may play in biology.

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“…13,14 There is now evidence that CDK5RAP2 homologues, C. elegans SPD-5 and Drosophila Cnn, are phase transitioning proteins, capable of assuming a solid aggregate or a liquid-like droplet form (Figure 3A). 15,31,62 …”

Section: Phase Transitions: Impact On Centrosomal Assembly and Functionmentioning

confidence: 99%

Phase Transitioning the Centrosome into a Microtubule Nucleator

2017

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Centrosomes are self-assembling, micron-scale, nonmembrane bound organelles that nucleate microtubules (MTs) and organize the microtubule cytoskeleton of the cell. They orchestrate critical cellular processes such as ciliary-based motility, vesicle trafficking, and cell division. Much is known about the role of the centrosome in these contexts, but we have a less comprehensive understanding of how the centrosome assembles and generates microtubules. Studies over the past 10 years have fundamentally shifted our view of these processes. Subdiffraction imaging has probed the amorphous haze of material surrounding the core of the centrosome revealing a complex, hierarchically organized structure whose composition and size changes profoundly during the transition from interphase to mitosis. New biophysical insights into protein phase transitions, where a diffuse protein spontaneously separates into a locally concentrated, nonmembrane bounded compartment, have provided a fresh perspective into how the centrosome might rapidly condense from diffuse cytoplasmic components. In this Perspective, we focus on recent findings that identify several centrosomal proteins that undergo phase transitions. We discuss how to reconcile these results with the current model of the underlying organization of proteins in the centrosome. Furthermore, we reflect on how these findings impact our understanding of how the centrosome undergoes self-assembly and promotes MT nucleation.

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The Eukaryotic CO2-Concentrating Organelle Is Liquid-like and Exhibits Dynamic Reorganization

Cited by 343 publications

References 78 publications

Physical Chemistry of Cellular Liquid‐Phase Separation

Physical Chemistry of Cellular Liquid‐Phase Separation

It Pays To Be in Phase

Phase Transitioning the Centrosome into a Microtubule Nucleator

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