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• W3092475374 abstract "The plant cell internal environment is a dynamic, intricate landscape composed of many intracellular compartments. Cells organize some cellular components through formation of biomolecular condensates—non-stoichiometric assemblies of protein and/or nucleic acids. In many cases, phase separation appears to either underly or contribute to the formation of biomolecular condensates. Many canonical membraneless compartments within animal cells form in a manner that is at least consistent with phase separation, including nucleoli, stress granules, Cajal bodies, and numerous additional bodies, regulated by developmental and environmental stimuli. In this Review, we examine the emerging roles for phase separation in plants. Further, drawing on studies carried out in other organisms, we identify cellular phenomenon in plants that might also arise via phase separation. We propose that plants make use of phase separation to a much greater extent than has been previously appreciated, implicating phase separation as an evolutionarily ancient mechanism for cellular organization. The plant cell internal environment is a dynamic, intricate landscape composed of many intracellular compartments. Cells organize some cellular components through formation of biomolecular condensates—non-stoichiometric assemblies of protein and/or nucleic acids. In many cases, phase separation appears to either underly or contribute to the formation of biomolecular condensates. Many canonical membraneless compartments within animal cells form in a manner that is at least consistent with phase separation, including nucleoli, stress granules, Cajal bodies, and numerous additional bodies, regulated by developmental and environmental stimuli. In this Review, we examine the emerging roles for phase separation in plants. Further, drawing on studies carried out in other organisms, we identify cellular phenomenon in plants that might also arise via phase separation. We propose that plants make use of phase separation to a much greater extent than has been previously appreciated, implicating phase separation as an evolutionarily ancient mechanism for cellular organization. Plants are exquisitely attuned to their environment, rapidly responding to alteration of light, temperature, soil nutrient composition, water status, and mechanical stimuli, among every conceivable alteration to their surroundings. Because plants are “born” (i.e., germinate) with a minimal set of organs, nearly all development occurs in response to these external stimuli, shaping the evolving and final form of the plant to achieve maximal productivity. These stimuli alter biochemical and transcriptional regimes within each cell to ultimately drive these developmental events. Process compartmentalization within a cell is integral to cellular function. In addition to “conventional” membrane-bound organelles, membraneless compartments composed of protein and/or RNA offer an additional mechanism for intracellular organization (Gomes and Shorter, 2019Gomes E. Shorter J. The molecular language of membraneless organelles.J. Biol. Chem. 2019; 294: 7115-7127Abstract Full Text Full Text PDF PubMed Scopus (98) Google Scholar). Historically, these compartments have been termed ribonucleoprotein (RNP) granules, cellular bodies, protein assemblies, or simply cellular aggregates. Recently, membraneless compartments have been collectively termed biomolecular condensates (or condensates for short) to describe their capacity to spatially concentrate biomolecules (Banani et al., 2017Banani S.F. Lee H.O. Hyman A.A. Rosen M.K. Biomolecular condensates: organizers of cellular biochemistry.Nat. Rev. Mol. Cell Biol. 2017; 18: 285-298Crossref PubMed Scopus (834) Google Scholar). It is important to emphasize we are using the term “biomolecular condensate” here in the manner in which it was originally defined: as a phenomenological descriptor for cases in which biomolecules are found to be spatially concentrated, without attribution of assembly mechanism, morphology, or material state. Liquid-liquid phase separation (LLPS) might underly formation of many different condensates (Hyman et al., 2014Hyman A.A. Weber C.A. Jülicher F. Liquid-liquid phase separation in biology.Annu. Rev. Cell Dev. Biol. 2014; 30: 39-58Crossref PubMed Google Scholar). LLPS describes a phenomenon whereby a solution demixes into two or more distinct phases that coexist with one another (reviewed in Boeynaems et al., 2018Boeynaems S. Alberti S. Fawzi N.L. Mittag T. Polymenidou M. Rousseau F. Schymkowitz J. Shorter J. Wolozin B. Van Den Bosch L. et al.Protein phase separation: a new phase in cell biology.Trends Cell Biol. 2018; 28: 420-435Abstract Full Text Full Text PDF PubMed Scopus (307) Google Scholar; Posey et al., 2018Posey A.E. Holehouse A.S. Pappu R.V. Phase separation of intrinsically disordered proteins.Methods Enzymol. 2018; 611: 1-30Crossref PubMed Scopus (27) Google Scholar; Gomes and Shorter, 2019Gomes E. Shorter J. The molecular language of membraneless organelles.J. Biol. Chem. 2019; 294: 7115-7127Abstract Full Text Full Text PDF PubMed Scopus (98) Google Scholar). To date the vast majority of studies examining the functions of various condensates as well as the underlying physical principles governing their formation have been carried out in fungal or animal systems. Studies examining phase separation in these systems have led to numerous breakthroughs in our understanding of fundamental cellular processes as well as underlying mechanisms driving disease (reviewed in Shin and Brangwynne, 2017Shin Y. Brangwynne C.P. Liquid phase condensation in cell physiology and disease.Science. 2017; 357: eaaf4382Crossref PubMed Scopus (559) Google Scholar; Boeynaems et al., 2018Boeynaems S. Alberti S. Fawzi N.L. Mittag T. Polymenidou M. Rousseau F. Schymkowitz J. Shorter J. Wolozin B. Van Den Bosch L. et al.Protein phase separation: a new phase in cell biology.Trends Cell Biol. 2018; 28: 420-435Abstract Full Text Full Text PDF PubMed Scopus (307) Google Scholar; Alberti et al., 2019Alberti S. Gladfelter A. Mittag T. Considerations and challenges in studying liquid-liquid phase separation and biomolecular condensates.Cell. 2019; 176: 419-434Abstract Full Text Full Text PDF PubMed Scopus (183) Google Scholar). In contrast, examination of phase separation in plant systems has been largely uninvestigated. Plants are subject to seasonal variance in environmental stressors and face unique challenges in their growth and development, which mgiht have led to evolution of plant-specific condensates that have yet to be discovered. Condensate formation is often sensitive to changes in temperature, pH, salt concentrations, and other parameters that fluctuate considerably throughout the life cycle of a plant, raising the possibility that plants might have had to adopt unique, plant-specific mechanisms to regulate condensate formation. Throughout the literature, multiple reports of protein localization are consistent with protein condensation within plant cells. In the nucleus, some examples include the nucleolus (Kalinina et al., 2018Kalinina N.O. Makarova S. Makhotenko A. Love A.J. Taliansky M. The multiple functions of the nucleolus in plant development, disease and stress responses.Front. Plant Sci. 2018; 9: 132Crossref PubMed Scopus (18) Google Scholar), Cajal bodies (Collier et al., 2006Collier S. Pendle A. Boudonck K. van Rij T. Dolan L. Shaw P. A distant coilin homologue is required for the formation of cajal bodies in Arabidopsis.Mol. Biol. Cell. 2006; 17: 2942-2951Crossref PubMed Scopus (0) Google Scholar), nuclear speckles (Reddy et al., 2012Reddy A.S. Day I.S. Göhring J. Barta A. Localization and dynamics of nuclear speckles in plants.Plant Physiol. 2012; 158: 67-77Crossref PubMed Scopus (47) Google Scholar), DNA damage foci (Rothkamm et al., 2015Rothkamm K. Barnard S. Moquet J. Ellender M. Rana Z. Burdak-Rothkamm S. DNA damage foci: meaning and significance.Environ. Mol. Mutagen. 2015; 56: 491-504Crossref PubMed Scopus (113) Google Scholar), dicing bodies (Liu et al., 2012Liu Q. Shi L. Fang Y. Dicing bodies.Plant Physiol. 2012; 158: 61-66Crossref PubMed Scopus (12) Google Scholar), and photobodies (Van Buskirk et al., 2012Van Buskirk E.K. Decker P.V. Chen M. Photobodies in light signaling.Plant Physiol. 2012; 158: 52-60Crossref PubMed Scopus (0) Google Scholar). In the cytoplasm, processing bodies (P-bodies) (Maldonado-Bonilla, 2014Maldonado-Bonilla L.D. Composition and function of P bodies in Arabidopsis thaliana.Front. Plant Sci. 2014; 5: 201Crossref PubMed Scopus (34) Google Scholar), stress granules (SGs) (Hamada et al., 2018Hamada T. Yako M. Minegishi M. Sato M. Kamei Y. Yanagawa Y. Toyooka K. Watanabe Y. Hara-Nishimura I. Stress granule formation is induced by a threshold temperature rather than a temperature difference in Arabidopsis.J. Cell Sci. 2018; 131Crossref Scopus (4) Google Scholar), and AUXIN RESPONSE FACTOR (ARF) bodies (Powers et al., 2019Powers S.K. Holehouse A.S. Korasick D.A. Schreiber K.H. Clark N.M. Jing H. Emenecker R. Han S. Tycksen E. Hwang I. et al.Nucleo-cytoplasmic partitioning of ARF proteins controls auxin responses in Arabidopsis thaliana.Mol. Cell. 2019; 76: 177-190.e5Abstract Full Text Full Text PDF PubMed Scopus (3) Google Scholar) are examples of condensates (Figure 1). In this review, we will first introduce basic concepts important for understanding biomolecular condensates and their relationship to phase separation. We then examine condensates found in plants that have been described as forming via phase separation in other systems and thus, we propose, might also from through phase separation in plants. We summarize the processes from the plant literature for which LLPS has been explicitly demonstrated or implicated, and we examine other plant-specific condensates that historically have been referred to by other names, including membraneless compartments, bodies, assemblies, or foci. Finally, we consider potential roles for phase separation in plants as well as the unique challenges that plants might face in regulating biomolecule compartmentalization via phase separation. In its most basic form, LLPS describes a phenomenon whereby under certain conditions a solution will spontaneously demix into two (or more) distinct solution phases that coexist with one another (reviewed in Boeynaems et al., 2018Boeynaems S. Alberti S. Fawzi N.L. Mittag T. Polymenidou M. Rousseau F. Schymkowitz J. Shorter J. Wolozin B. Van Den Bosch L. et al.Protein phase separation: a new phase in cell biology.Trends Cell Biol. 2018; 28: 420-435Abstract Full Text Full Text PDF PubMed Scopus (307) Google Scholar; Posey et al., 2018Posey A.E. Holehouse A.S. Pappu R.V. Phase separation of intrinsically disordered proteins.Methods Enzymol. 2018; 611: 1-30Crossref PubMed Scopus (27) Google Scholar; Gomes and Shorter, 2019Gomes E. Shorter J. The molecular language of membraneless organelles.J. Biol. Chem. 2019; 294: 7115-7127Abstract Full Text Full Text PDF PubMed Scopus (98) Google Scholar). For example, in a simple in vitro system of buffer and protein, these two phases appear as a dense protein-rich spherical droplet surrounded by a dilute protein-poor solution. Demixing depends on the total concentration of the protein as well as other parameters that define the state of the system (temperature, solution ions, pH, etc.) (Figure 2A). Upon demixing of a simple two-component system, any additional protein molecules introduced are recruited into the dense phase, which also experiences a corresponding (albeit small) increase in volume. Consequently, for a simple two-component system, as the total protein concentration increases the concentration of protein in each of the two phases remains fixed, and the volume of the dense phase increases while the volume of the dilute phase decreases (Figure 2A) (reviewed in Holehouse, 2019Holehouse A.S. Chapter 7 -- IDPs and IDRs in biomolecular condensates.in: Salvi N. Intrinsically Disordered Proteins. Academic Press, 2019: 209-255Crossref Google Scholar). In cells, the formation of membraneless compartments through LLPS will almost always involve many different components, such that although we expect the same class of physical principles to underlie both in vitro and in vivo assembly, some of the limiting behaviors observed for a simple protein and buffer systems might no longer be applicable (Choi et al., 2019Choi J.M. Dar F. Pappu R.V. LASSI: a lattice model for simulating phase transitions of multivalent proteins.PLoS Comput. Biol. 2019; 15: e1007028Crossref PubMed Scopus (21) Google Scholar; Riback et al., 2020Riback J.A. Zhu L. Ferrolino M.C. Tolbert M. Mitrea D.M. Sanders D.W. Wei M.-T. Kriwacki R.W. Brangwynne C.P. Composition-dependent thermodynamics of intracellular phase separation.Nature. 2020; 581: 209-214Crossref PubMed Scopus (0) Google Scholar). Non-stoichiometric phase-separated assemblies composed of proteins or proteins and nucleic acids have been termed “biomolecular condensates” (or just “condensates”) to describe their capacity to concentrate biomolecules (Banani et al., 2017Banani S.F. Lee H.O. Hyman A.A. Rosen M.K. Biomolecular condensates: organizers of cellular biochemistry.Nat. Rev. Mol. Cell Biol. 2017; 18: 285-298Crossref PubMed Scopus (834) Google Scholar). Unequivocally demonstrating that condensates form via LLPS in vivo can be challenging because of the inherently complex and out-of-equilibrium nature of the cellular environment (McSwiggen et al., 2019McSwiggen D.T. Mir M. Darzacq X. Tjian R. Evaluating phase separation in live cells: diagnosis, caveats, and functional consequences.Genes Dev. 2019; 33: 1619-1634Crossref PubMed Scopus (29) Google Scholar). However, many proteins that form condensates demonstrably undergo LLPS in vitro and do so in a manner that recapitulates features of their cellular behavior, and in vitro characterization allows for the identification of mutations that alter in vivo assembly and are predictive of augmented cellular function (Riback et al., 2017Riback J.A. Katanski C.D. Kear-Scott J.L. Pilipenko E.V. Rojek A.E. Sosnick T.R. Drummond D.A. Stress-triggered phase separation is an adaptive, evolutionarily tuned response.Cell. 2017; 168: 1028-1040.e19Abstract Full Text Full Text PDF PubMed Scopus (193) Google Scholar). Altogether, these types of integrative studies support the notion that LLPS might be the underlying process that drives condensate formation, or at least that the same physical interactions that drive LLPS in vitro mediate assembly in vivo in a predictive way but via some other as-of-yet undetermined mechanism (Holehouse, 2019Holehouse A.S. Chapter 7 -- IDPs and IDRs in biomolecular condensates.in: Salvi N. Intrinsically Disordered Proteins. Academic Press, 2019: 209-255Crossref Google Scholar). The dynamics, morphology, and internal structure of condensates are a complex set of topics that have been reviewed extensively elsewhere (reviewed in Hyman et al., 2014Hyman A.A. Weber C.A. Jülicher F. Liquid-liquid phase separation in biology.Annu. Rev. Cell Dev. Biol. 2014; 30: 39-58Crossref PubMed Google Scholar; Weber, 2017Weber S.C. Sequence-encoded material properties dictate the structure and function of nuclear bodies.Curr. Opin. Cell Biol. 2017; 46: 62-71Crossref PubMed Scopus (28) Google Scholar; Woodruff et al., 2018Woodruff J.B. Hyman A.A. Boke E. Organization and function of non-dynamic biomolecular condensates.Trends Biochem. Sci. 2018; 43: 81-94Abstract Full Text Full Text PDF PubMed Scopus (37) Google Scholar; Alberti et al., 2019Alberti S. Gladfelter A. Mittag T. Considerations and challenges in studying liquid-liquid phase separation and biomolecular condensates.Cell. 2019; 176: 419-434Abstract Full Text Full Text PDF PubMed Scopus (183) Google Scholar; Peran and Mittag, 2020Peran I. Mittag T. Molecular structure in biomolecular condensates.Curr. Opin. Struct. Biol. 2020; 60: 17-26Crossref PubMed Scopus (2) Google Scholar). One important concept that we emphasize is that a wide variety of condensate material properties are compatible with biological function, such that condensates that apparently form via LLPS need not retain liquid-like properties. At its core, condensate formation through LLPS relies on molecules with the capacity to form many interactions, a property referred to as multivalency (reviewed in Banani et al., 2017Banani S.F. Lee H.O. Hyman A.A. Rosen M.K. Biomolecular condensates: organizers of cellular biochemistry.Nat. Rev. Mol. Cell Biol. 2017; 18: 285-298Crossref PubMed Scopus (834) Google Scholar). Multivalency can be found in many biologically relevant molecules such as proteins and RNA. Multivalent molecules contain many modules that can facilitate inter- and intramolecular interactions with multiple partners, a feature integral to their ability to phase separate and form condensates (Harmon et al., 2017Harmon T.S. Holehouse A.S. Rosen M.K. Pappu R.V. Intrinsically disordered linkers determine the interplay between phase separation and gelation in multivalent proteins.eLife. 2017; 6: e30294Crossref PubMed Google Scholar). Multivalency is well described by the “stickers and spacers mode” of associative polymers, originally introduced by Semenov and Rubinstein and more recently applied to biological polymers (reviewed in Choi et al., 2020Choi S.W. Ryu M.Y. Viczián A. Jung H.J. Kim G.M. Arce A.L. Achkar N.P. Manavella P. Dolde U. Wenkel S. et al.Light triggers the miRNA-biogenetic inconsistency for de-etiolated seedling survivability in Arabidopsis thaliana.Mol. Plant. 2020; 13: 431-445Abstract Full Text Full Text PDF Scopus (3) Google Scholar, Choi et al., 2019Choi J.M. Dar F. Pappu R.V. LASSI: a lattice model for simulating phase transitions of multivalent proteins.PLoS Comput. Biol. 2019; 15: e1007028Crossref PubMed Scopus (21) Google Scholar; Rubinstein and Dobrynin, 1997Rubinstein M. Dobrynin A.V. Solutions of associative polymers.Trends Polym. Sci. 1997; 5: 181-186Google Scholar; Semenov and Rubinstein, 1998Semenov A.N. Rubinstein M. Thermoreversible gelation in solutions of associative polymers.Macromolecules. 1998; 31: 1373-1385Crossref Google Scholar; Wang et al., 2018Wang J. Choi J.M. Holehouse A.S. Lee H.O. Zhang X. Jahnel M. Maharana S. Lemaitre R. Pozniakovsky A. Drechsel D. et al.A molecular grammar governing the driving forces for phase separation of prion-like RNA binding proteins.Cell. 2018; 174: 688-699.e16Abstract Full Text Full Text PDF PubMed Scopus (235) Google Scholar). Stickers refer to molecular regions that mediate attractive intermolecular interactions and can be encoded by various different molecular features including binding sites on the surface of folded domains, binding domains connected in tandem by disordered linkers, or short linear motifs embedded within intrinsically disordered regions (IDRs) (Figure 2B) (reviewed in Banani et al., 2017Banani S.F. Lee H.O. Hyman A.A. Rosen M.K. Biomolecular condensates: organizers of cellular biochemistry.Nat. Rev. Mol. Cell Biol. 2017; 18: 285-298Crossref PubMed Scopus (834) Google Scholar; Posey et al., 2018Posey A.E. Holehouse A.S. Pappu R.V. Phase separation of intrinsically disordered proteins.Methods Enzymol. 2018; 611: 1-30Crossref PubMed Scopus (27) Google Scholar). IDRs are protein regions that exist in an ensemble or “cloud” of interconverting conformations, as opposed to adopting a fixed tertiary structure (reviewed in Oldfield and Dunker, 2014Oldfield C.J. Dunker A.K. Intrinsically disordered proteins and intrinsically disordered protein regions.Annu. Rev. Biochem. 2014; 83: 553-584Crossref PubMed Scopus (390) Google Scholar). IDRs have garnered much attention in the context of condensates because in a number of systems they are necessary and sufficient to drive phase separation in vitro (reviewed in Holehouse, 2019Holehouse A.S. Chapter 7 -- IDPs and IDRs in biomolecular condensates.in: Salvi N. Intrinsically Disordered Proteins. Academic Press, 2019: 209-255Crossref Google Scholar). However, we emphasize that IDRs are not special, and although they might provide a physiologically convenient platform upon which multivalency can be encoded, IDRs do not drive phase separation, multivalency does. Whereas an individual binding motif on a disordered region might be weak, it is important to remember that IDRs do not necessarily confer weak binding, just as folded domains do not necessarily confer strong binding (Borgia et al., 2018Borgia A. Borgia M.B. Bugge K. Kissling V.M. Heidarsson P.O. Fernandes C.B. Sottini A. Soranno A. Buholzer K.J. Nettels D. et al.Extreme disorder in an ultrahigh-affinity protein complex.Nature. 2018; 555: 61-66Crossref PubMed Scopus (180) Google Scholar). One conceptually appealing model for describing condensates in vivo is the scaffold and client model (Banani et al., 2016Banani S.F. Rice A.M. Peeples W.B. Lin Y. Jain S. Parker R. Rosen M.K. Compositional control of phase-separated cellular bodies.Cell. 2016; 166: 651-663Abstract Full Text Full Text PDF PubMed Scopus (249) Google Scholar). Here, multivalent molecules (protein or RNA) that are necessary for the formation of a condensate are termed the scaffolds (reviewed in Posey et al., 2018Posey A.E. Holehouse A.S. Pappu R.V. Phase separation of intrinsically disordered proteins.Methods Enzymol. 2018; 611: 1-30Crossref PubMed Scopus (27) Google Scholar). It is worth noting that scaffold molecules do not necessarily drive condensate formation in isolation; rather they are necessary but not necessarily sufficient for a given condensate of interest. This is in contrast to “client” molecules, which preferentially localize to the condensate but are neither necessary nor sufficient for its assembly (Banani et al., 2017Banani S.F. Lee H.O. Hyman A.A. Rosen M.K. Biomolecular condensates: organizers of cellular biochemistry.Nat. Rev. Mol. Cell Biol. 2017; 18: 285-298Crossref PubMed Scopus (834) Google Scholar). Although convenient, the scaffold-client model has some limitations if interpreted without care. Clients that partition into condensates will still alter condensate behavior to an extent that is related to the strength with which they partition and the mode in which they interact with the condensate components, giving rise to complex and potentially counterintuitive behavior (Choi et al., 2019Choi J.M. Dar F. Pappu R.V. LASSI: a lattice model for simulating phase transitions of multivalent proteins.PLoS Comput. Biol. 2019; 15: e1007028Crossref PubMed Scopus (21) Google Scholar; Riback et al., 2020Riback J.A. Zhu L. Ferrolino M.C. Tolbert M. Mitrea D.M. Sanders D.W. Wei M.-T. Kriwacki R.W. Brangwynne C.P. Composition-dependent thermodynamics of intracellular phase separation.Nature. 2020; 581: 209-214Crossref PubMed Scopus (0) Google Scholar; Ruff et al., 2020Ruff K. Dar F. Pappu R. Ligand effects on phase separation of multivalent macromolecules.bioRxiv. 2020; https://www.biorxiv.org/content/10.1101/2020.08.15.252346v1#:∼:text=In%20contrast%2C%20multivalent%20ligands%2C%20depending,are%20generally%20diluted%20by%20ligandsGoogle Scholar). An emerging function of condensates is their ability to act as a means for dynamic cellular response to the environment that can be regulated in various ways. Mounting evidence supports IDR post-translational modification as a mechanism to regulate phase separation propensity (reviewed in Owen and Shewmaker, 2019Owen I. Shewmaker F. The role of post-translational modifications in the phase transitions of intrinsically disordered proteins.Int. J. Mol. Sci. 2019; 20Crossref Scopus (7) Google Scholar), highlighting the potential for condensate formation to be a dynamic process. Indeed, many condensates form in response to specific stimuli such as changes in nutrient availability, pH, or temperature (reviewed in Yoo et al., 2019Yoo H. Triandafillou C. Drummond D.A. Cellular sensing by phase separation: using the process, not just the products.J. Biol. Chem. 2019; 294: 7151-7159Abstract Full Text Full Text PDF PubMed Scopus (0) Google Scholar), all of which are critical drivers of plant development. Apart from the capacity of condensates to dynamically assemble and disassemble, potential functional benefits to condensate formation include sequestering or concentrating molecules involved in a specific process or buffering the concentration of a molecule (reviewed in Holehouse and Pappu, 2018Holehouse A.S. Pappu R.V. Functional implications of intracellular phase transitions.Biochemistry. 2018; 57: 2415-2423Crossref PubMed Scopus (54) Google Scholar). The plant literature contains many cellular bodies that fit the definition of a condensate (Table 1); however, these have historically been described by using distinct language and terminology. As a reminder, a condensate here refers simply to cases in which biomolecules are found to be spatially concentrated but makes no assumption regarding the assembly mechanism, the morphology, or the material properties of those assemblies. Some plant-based condensates represent “classic” membraneless organelles as observed in animals, whereas others are more specialized and might represent plant or species-specific cellular bodies. Given the burgeoning field of biomolecular condensates in other systems, we propose the same set of language can be used to classify and describe cellular bodies in plants that had previously appeared under a variety of names. This common language allows us to ask questions in plants in which previously characterized bodies (condensates) might be re-evaluated in the context of a new emerging field of cellular organization.Table 1Comparing Biomolecular Condensates between Plants and AnimalsCellular LocalizationPresence in Plants or AnimalsBiomolecular CondensateFunctionNucleusP, AnucleolusrRNA biosynthesis and ribosome biogenesis (reviewed in Kalinina et al., 2018Kalinina N.O. Makarova S. Makhotenko A. Love A.J. Taliansky M. The multiple functions of the nucleolus in plant development, disease and stress responses.Front. Plant Sci. 2018; 9: 132Crossref PubMed Scopus (18) Google Scholar)nuclear specklesconcentrates RNA metabolism factors involved (reviewed in Spector and Lamond, 2011Spector D.L. Lamond A.I. Nuclear speckles.Cold Spring Harb. Perspect. Biol. 2011; 3: a000646Crossref PubMed Scopus (377) Google Scholar)cajal bodiesmRNA metabolism and snRNP biogenesis (reviewed in Ohtani, 2017Ohtani M. Plant snRNP biogenesis: a perspective from the nucleolus and Cajal bodies.Front. Plant Sci. 2017; 8: 2184Crossref Scopus (6) Google Scholar)DNA damage fociconcentrates DNA response proteins (reviewed in Rothkamm et al., 2015Rothkamm K. Barnard S. Moquet J. Ellender M. Rana Z. Burdak-Rothkamm S. DNA damage foci: meaning and significance.Environ. Mol. Mutagen. 2015; 56: 491-504Crossref PubMed Scopus (113) Google Scholar)Pphotobodiesconcentrates light signaling proteins (reviewed in Ronald and Davis, 2019Ronald J. Davis S.J. Focusing on the nuclear and subnuclear dynamics of light and circadian signalling.Plant Cell Environ. 2019; 42: 2871-2884Crossref Scopus (3) Google Scholar)dicing bodiesmiRNA processing (reviewed in Liu et al., 2012Liu Q. Shi L. Fang Y. Dicing bodies.Plant Physiol. 2012; 158: 61-66Crossref PubMed Scopus (12) Google Scholar)Aparaspecklesgene expression regulation by sequestering RNA or proteins (reviewed in Fox et al., 2018Fox A.H. Nakagawa S. Hirose T. Bond C.S. Paraspeckles: where long noncoding RNA meets phase separation.Trends Biochem. Sci. 2018; 43: 124-135Abstract Full Text Full Text PDF PubMed Scopus (88) Google Scholar)histone locus bodiesprocessing histone pre-mRNAs (reviewed in Nizami et al., 2010Nizami Z. Deryusheva S. Gall J.G. The Cajal body and histone locus body.Cold Spring Harb. Perspect. Biol. 2010; 2: a000653Crossref PubMed Scopus (136) Google Scholar)PcG bodyrepression of genes related to development (reviewed in Pirrotta and Li, 2012Pirrotta V. Li H.B. A view of nuclear polycomb bodies.Curr. Opin. Genet. Dev. 2012; 22: 101-109Crossref PubMed Scopus (93) Google Scholar)PML bodygenome integrity preservation during DNA synthesis (reviewed in Li et al., 2020Li Y. Ma X. Wu W. Chen Z. Meng G. PML nuclear body biogenesis, carcinogenesis, and targeted therapy.Trends Cancer. 2020; https://doi.org/10.1016/j.trecan.2020.05.005Abstract Full Text Full Text PDF Scopus (0) Google Scholar)nuclear gemSMN complex component localization (reviewed in Gubitz et al., 2004Gubitz A.K. Feng W. Dreyfuss G. The SMN complex.Exp. Cell Res. 2004; 296: 51-56Crossref PubMed Scopus (197) Google Scholar)CytoplasmP, Aprocessing bodymRNA decay and suppression of translation (reviewed in Luo et al., 2018Luo Y. Na Z. Slavoff S.A. P-bodies: composition, properties, and functions.Biochemistry. 2018; 57: 2424-2431Crossref PubMed Scopus (58) Google Scholar)stress granuletranslation suppression during stress responses (reviewed in Protter and Parker, 2016Protter D.S.W. Parker R. Principles and properties of stress granules.Trends Cell Biol. 2016; 26: 668-679Abstract Full Text Full Text PDF PubMed Scopus (360) Google Scholar)AU bodyassembly and storage of snRNPs (reviewed in Moser and Fritzler, 2010Moser J.J. Fritzler M.J. Cytoplasmic ribonucleoprotein (RNP) bodies and their relationship to GW/P bodies.Int. J. Biochem. Cell Biol. 2010; 42: 828-843Crossref PubMed Scopus (56) Google Scholar)germ granuleregulation of mRNA translation during germ cell development (reviewed in Trcek and Lehmann, 2017Trcek T. Lehmann R. All about the RNA after all.eLife. 2017; 6Crossref Scopus (3) Google Scholar)balbiani bodyelimination of dysfunctional mitochondria from germline cells (reviewed in Bilinski et al., 2017Bilinski S.M. Kloc M. Tworzydlo W. Selection of mitochondria in female germline cells: is Balbiani body implicated in this process?.J. Assist. Reprod. Genet. 2017; 34: 1405-1412Crossref PubMed Scopus (17) Google Scholar) and to preserve mitochondria d" @default.
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• W3092475374 title "Emerging Roles for Phase Separation in Plants" @default.
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