Sequence Determinants of Intracellular Phase Separation by Complex Coacervation of a Disordered Protein
Liquid-liquid phase separation, driven by collective interactions among multivalent and intrinsically disordered proteins, is thought to mediate the formation of membrane-less organelles in cells. Using parallel cellular and in vitro assays, we show that the Nephrin intracellular domain (NICD), a di...
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| Published in | Molecular cell Vol. 63; no. 1; pp. 72 - 85 |
|---|---|
| Main Authors | , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
07.07.2016
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Liquid-liquid phase separation, driven by collective interactions among multivalent and intrinsically disordered proteins, is thought to mediate the formation of membrane-less organelles in cells. Using parallel cellular and in vitro assays, we show that the Nephrin intracellular domain (NICD), a disordered protein, drives intracellular phase separation via complex coacervation, whereby the negatively charged NICD co-assembles with positively charged partners to form protein-rich dense liquid droplets. Mutagenesis reveals that the driving force for phase separation depends on the overall amino acid composition and not the precise sequence of NICD. Instead, phase separation is promoted by one or more regions of high negative charge density and aromatic/hydrophobic residues that are distributed across the protein. Many disordered proteins share similar sequence characteristics with NICD, suggesting that complex coacervation may be a widely used mechanism to promote intracellular phase separation.
[Display omitted]
•Disordered Nephrin intracellular domain (NICD) forms phase-separated nuclear bodies•NICD phase separates via complex coacervation•Aromatic/hydrophobic residues and high (−) charge density promote phase separation•Disordered regions with NICD-like sequence features are common in human proteome
Pak et al. describe cellular liquid-liquid phase separation of a negatively charged intrinsically disordered protein, the Nephrin intracellular domain. Phase separation is driven by co-assembly with positively charged partners, a process termed complex coacervation. Disordered regions with NICD-like sequence features are common in the human proteome, suggesting complex coacervation may be widespread. |
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| AbstractList | Liquid-liquid phase separation, driven by collective interactions among multivalent and intrinsically disordered proteins, is thought to mediate the formation of membrane-less organelles in cells. Using parallel cellular and in vitro assays, we show that the Nephrin intracellular domain (NICD), a disordered protein, drives intracellular phase separation via complex coacervation, whereby the negatively charged NICD co-assembles with positively charged partners to form protein-rich dense liquid droplets. Mutagenesis reveals that the driving force for phase separation depends on the overall amino acid composition and not the precise sequence of NICD. Instead, phase separation is promoted by one or more regions of high negative charge density and aromatic/hydrophobic residues that are distributed across the protein. Many disordered proteins share similar sequence characteristics with NICD, suggesting that complex coacervation may be a widely used mechanism to promote intracellular phase separation. Liquid-liquid phase separation, driven by collective interactions among multivalent and intrinsically disordered proteins, is thought to mediate the formation of membrane-less organelles in cells. Using parallel cellular and in vitro assays, we show that the Nephrin intracellular domain (NICD), a disordered protein, drives intracellular phase separation via complex coacervation, whereby the negatively charged NICD co-assembles with positively charged partners to form protein-rich dense liquid droplets. Mutagenesis reveals that the driving force for phase separation depends on the overall amino acid composition and not the precise sequence of NICD. Instead, phase separation is promoted by one or more regions of high negative charge density and aromatic/hydrophobic residues that are distributed across the protein. Many disordered proteins share similar sequence characteristics with NICD, suggesting that complex coacervation may be a widely used mechanism to promote intracellular phase separation.Liquid-liquid phase separation, driven by collective interactions among multivalent and intrinsically disordered proteins, is thought to mediate the formation of membrane-less organelles in cells. Using parallel cellular and in vitro assays, we show that the Nephrin intracellular domain (NICD), a disordered protein, drives intracellular phase separation via complex coacervation, whereby the negatively charged NICD co-assembles with positively charged partners to form protein-rich dense liquid droplets. Mutagenesis reveals that the driving force for phase separation depends on the overall amino acid composition and not the precise sequence of NICD. Instead, phase separation is promoted by one or more regions of high negative charge density and aromatic/hydrophobic residues that are distributed across the protein. Many disordered proteins share similar sequence characteristics with NICD, suggesting that complex coacervation may be a widely used mechanism to promote intracellular phase separation. Liquid-liquid phase separation, driven by collective interactions among multivalent and intrinsically disordered proteins, is thought to mediate the formation of membrane-less organelles in cells. Using parallel cellular and in vitro assays we show that the Nephrin intracellular domain (NICD), a disordered protein, drives intracellular phase separation via complex coacervation, whereby the negatively charged NICD co-assembles with positively charged partners to form protein-rich dense liquid droplets. Mutagenesis reveals that the driving force for phase separation depends on the overall amino acid composition and not the precise sequence of NICD. Instead, phase separation is promoted by one or more regions of high negative charge density and aromatic/hydrophobic residues that are distributed across the protein. Many disordered proteins share similar sequence characteristics with NICD, suggesting that complex coacervation may be a widely used mechanism to promote intracellular phase separation. Liquid-liquid phase separation, driven by collective interactions among multivalent and intrinsically disordered proteins, is thought to mediate the formation of membrane-less organelles in cells. Using parallel cellular and in vitro assays, we show that the Nephrin intracellular domain (NICD), a disordered protein, drives intracellular phase separation via complex coacervation, whereby the negatively charged NICD co-assembles with positively charged partners to form protein-rich dense liquid droplets. Mutagenesis reveals that the driving force for phase separation depends on the overall amino acid composition and not the precise sequence of NICD. Instead, phase separation is promoted by one or more regions of high negative charge density and aromatic/hydrophobic residues that are distributed across the protein. Many disordered proteins share similar sequence characteristics with NICD, suggesting that complex coacervation may be a widely used mechanism to promote intracellular phase separation. [Display omitted] •Disordered Nephrin intracellular domain (NICD) forms phase-separated nuclear bodies•NICD phase separates via complex coacervation•Aromatic/hydrophobic residues and high (−) charge density promote phase separation•Disordered regions with NICD-like sequence features are common in human proteome Pak et al. describe cellular liquid-liquid phase separation of a negatively charged intrinsically disordered protein, the Nephrin intracellular domain. Phase separation is driven by co-assembly with positively charged partners, a process termed complex coacervation. Disordered regions with NICD-like sequence features are common in the human proteome, suggesting complex coacervation may be widespread. Liquid-liquid phase separation, driven by collective interactions among multivalent and intrinsically disordered proteins, is thought to mediate the formation of membrane-less organelles in cells. Using parallel cellular and in vitro assays, we show that the Nephrin intracellular domain (NICD), a disordered protein, drives intracellular phase separation via complex coacervation, whereby the negatively charged NICD co-assembles with positively charged partners to form protein-rich dense liquid droplets. Mutagenesis reveals that the driving force for phase separation depends on the overall amino acid composition and not the precise sequence of NICD. Instead, phase separation is promoted by one or more regions of high negative charge density and aromatic/hydrophobic residues that are distributed across the protein. Many disordered proteins share similar sequence characteristics with NICD, suggesting that complex coacervation may be a widely used mechanism to promote intracellular phase separation. |
| Author | Pak, Chi W. Liu, David R. Holehouse, Alex S. Mittal, Anuradha Yunus, Ali A. Pappu, Rohit V. Padrick, Shae B. Kosno, Martyna Rosen, Michael K. Ali, Rustam |
| AuthorAffiliation | 1 Department of Biophysics and Howard Hughes Medical Institute, UT Southwestern Medical Center, Dallas, TX, 75390, USA 3 Department of Biomedical Engineering and Center for Biological Systems Engineering, Washington University in St. Louis, St. Louis, Missouri, 63130, USA 4 Department of Chemistry and Chemical Biology and Howard Hughes Medical Institute, Harvard University, Cambridge, Massachusetts, 02138, USA 2 Computational and Molecular Biophysics Graduate Program, Washington University in St. Louis, St. Louis, Missouri, 63130, USA |
| AuthorAffiliation_xml | – name: 2 Computational and Molecular Biophysics Graduate Program, Washington University in St. Louis, St. Louis, Missouri, 63130, USA – name: 1 Department of Biophysics and Howard Hughes Medical Institute, UT Southwestern Medical Center, Dallas, TX, 75390, USA – name: 4 Department of Chemistry and Chemical Biology and Howard Hughes Medical Institute, Harvard University, Cambridge, Massachusetts, 02138, USA – name: 3 Department of Biomedical Engineering and Center for Biological Systems Engineering, Washington University in St. Louis, St. Louis, Missouri, 63130, USA |
| Author_xml | – sequence: 1 givenname: Chi W. surname: Pak fullname: Pak, Chi W. organization: Department of Biophysics and Howard Hughes Medical Institute, UT Southwestern Medical Center, Dallas, TX 75390, USA – sequence: 2 givenname: Martyna surname: Kosno fullname: Kosno, Martyna organization: Department of Biophysics and Howard Hughes Medical Institute, UT Southwestern Medical Center, Dallas, TX 75390, USA – sequence: 3 givenname: Alex S. surname: Holehouse fullname: Holehouse, Alex S. organization: Computational and Molecular Biophysics Graduate Program, Washington University in St. Louis, St. Louis, MO 63130, USA – sequence: 4 givenname: Shae B. surname: Padrick fullname: Padrick, Shae B. organization: Department of Biophysics and Howard Hughes Medical Institute, UT Southwestern Medical Center, Dallas, TX 75390, USA – sequence: 5 givenname: Anuradha surname: Mittal fullname: Mittal, Anuradha organization: Department of Biomedical Engineering and Center for Biological Systems Engineering, Washington University in St. Louis, St. Louis, MO 63130, USA – sequence: 6 givenname: Rustam surname: Ali fullname: Ali, Rustam organization: Department of Biophysics and Howard Hughes Medical Institute, UT Southwestern Medical Center, Dallas, TX 75390, USA – sequence: 7 givenname: Ali A. surname: Yunus fullname: Yunus, Ali A. organization: Department of Biophysics and Howard Hughes Medical Institute, UT Southwestern Medical Center, Dallas, TX 75390, USA – sequence: 8 givenname: David R. surname: Liu fullname: Liu, David R. organization: Department of Chemistry and Chemical Biology and Howard Hughes Medical Institute, Harvard University, Cambridge, MA 02138, USA – sequence: 9 givenname: Rohit V. surname: Pappu fullname: Pappu, Rohit V. email: pappu@wustl.edu organization: Department of Biomedical Engineering and Center for Biological Systems Engineering, Washington University in St. Louis, St. Louis, MO 63130, USA – sequence: 10 givenname: Michael K. surname: Rosen fullname: Rosen, Michael K. email: michael.rosen@utsouthwestern.edu organization: Department of Biophysics and Howard Hughes Medical Institute, UT Southwestern Medical Center, Dallas, TX 75390, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/27392146$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1038/nrm3920 10.1038/nature04662 10.1093/nar/gku982 10.1073/pnas.1017150108 10.1073/pnas.1504822112 10.1002/jcc.21005 10.1016/j.cell.2015.08.010 10.1146/annurev-cellbio-100913-013325 10.1016/j.cell.2015.09.015 10.1093/nar/gks1118 10.1016/j.cell.2012.04.017 10.1093/hmg/dds116 10.7554/eLife.06807 10.1016/j.molcel.2015.08.018 10.1002/anie.201402885 10.1126/science.1172046 10.1016/j.molcel.2015.09.006 10.7554/eLife.04123 10.1073/pnas.0807883106 10.1016/j.molcel.2015.09.017 10.1016/j.bpj.2014.11.1260 10.1038/nature10879 10.7554/eLife.04591 10.1073/pnas.1304749110 10.1073/pnas.1509317112 10.1016/j.molcel.2015.01.013 10.1074/jbc.M308465200 10.1016/j.cell.2006.11.026 10.1073/pnas.1508778112 10.1038/nphys3532 10.1016/j.cell.2012.04.016 10.1016/j.cell.2015.07.047 10.1016/j.cis.2011.01.007 10.1016/j.cell.2015.10.040 10.1016/j.molcel.2009.01.026 |
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| References | Burke, Janke, Rhine, Fawzi (bib7) 2015; 60 Banjade, Wu, Mittal, Peeples, Pappu, Rosen (bib2) 2015; 112 Berry, Weber, Vaidya, Haataja, Brangwynne (bib3) 2015; 112 Hyman, Weber, Jülicher (bib16) 2014; 30 Elbaum-Garfinkle, Kim, Szczepaniak, Chen, Eckmann, Myong, Brangwynne (bib12) 2015; 112 Brangwynne, Eckmann, Courson, Rybarska, Hoege, Gharakhani, Jülicher, Hyman (bib4) 2009; 324 Brangwynne, Tompa, Pappu (bib6) 2015; 11 Jones, Blasutig, Eremina, Ruston, Bladt, Li, Huang, Larose, Li, Takano (bib18) 2006; 440 Spector (bib30) 2006; 127 Das, Pappu (bib10) 2013; 110 Molliex, Temirov, Lee, Coughlin, Kanagaraj, Kim, Mittag, Taylor (bib26) 2015; 163 Nott, Petsalaki, Farber, Jervis, Fussner, Plochowietz, Craggs, Bazett-Jones, Pawson, Forman-Kay, Baldwin (bib27) 2015; 57 Brangwynne, Mitchison, Hyman (bib5) 2011; 108 Wang, Smith, Chen, Schmidt, Rasoloson, Paix, Lambrus, Calidas, Betzig, Seydoux (bib33) 2014; 3 McNaughton, Cronican, Thompson, Liu (bib23) 2009; 106 Zhang, Elbaum-Garfinkle, Langdon, Taylor, Occhipinti, Bridges, Brangwynne, Gladfelter (bib36) 2015; 60 Xiang, Kato, Wu, Lin, Ding, Zhang, Yu, McKnight (bib35) 2015; 163 Vitalis, Pappu (bib32) 2009; 30 Kato, Han, Xie, Shi, Du, Wu, Mirzaei, Goldsmith, Longgood, Pei (bib19) 2012; 149 Wright, Dyson (bib34) 2015; 16 Holehouse, Ahad, Das, Pappu (bib15) 2015; 108 Fromm, Kamenz, Nöldeke, Neu, Zocher, Sprangers (bib13) 2014; 53 Han, Kato, Xie, Wu, Mirzaei, Pei, Chen, Xie, Allen, Xiao, McKnight (bib14) 2012; 149 Li, Banjade, Cheng, Kim, Chen, Guo, Llaguno, Hollingsworth, King, Banani (bib21) 2012; 483 Patel, Lee, Jawerth, Maharana, Jahnel, Hein, Stoynov, Mahamid, Saha, Franzmann (bib28) 2015; 162 Lin, Protter, Rosen, Parker (bib22) 2015; 60 Jiang, Wang, Huang, He, Cui, Zhu, Zheng (bib17) 2015; 163 Potenza, Di Domenico, Walsh, Tosatto (bib29) 2015; 43 Mi, Muruganujan, Thomas (bib24) 2013; 41 Veis (bib31) 2011; 167 Couthouis, Hart, Erion, King, Diaz, Nakaya, Ibrahim, Kim, Mojsilovic-Petrovic, Panossian (bib9) 2012; 21 Kroschwald, Maharana, Mateju, Malinovska, Nüske, Poser, Richter, Alberti (bib20) 2015; 4 Banjade, Rosen (bib1) 2014; 3 Dill, Bromberg (bib11) 2010 Miao, Bellingham, Stahl, Sitarz, Lane, Keeley (bib25) 2003; 278 Clemson, Hutchinson, Sara, Ensminger, Fox, Chess, Lawrence (bib8) 2009; 33 Elbaum-Garfinkle (10.1016/j.molcel.2016.05.042_bib12) 2015; 112 Banjade (10.1016/j.molcel.2016.05.042_bib2) 2015; 112 Clemson (10.1016/j.molcel.2016.05.042_bib8) 2009; 33 Miao (10.1016/j.molcel.2016.05.042_bib25) 2003; 278 Holehouse (10.1016/j.molcel.2016.05.042_bib15) 2015; 108 Kato (10.1016/j.molcel.2016.05.042_bib19) 2012; 149 Molliex (10.1016/j.molcel.2016.05.042_bib26) 2015; 163 Li (10.1016/j.molcel.2016.05.042_bib21) 2012; 483 Veis (10.1016/j.molcel.2016.05.042_bib31) 2011; 167 Potenza (10.1016/j.molcel.2016.05.042_bib29) 2015; 43 Couthouis (10.1016/j.molcel.2016.05.042_bib9) 2012; 21 Spector (10.1016/j.molcel.2016.05.042_bib30) 2006; 127 Das (10.1016/j.molcel.2016.05.042_bib10) 2013; 110 Mi (10.1016/j.molcel.2016.05.042_bib24) 2013; 41 Xiang (10.1016/j.molcel.2016.05.042_bib35) 2015; 163 Wright (10.1016/j.molcel.2016.05.042_bib34) 2015; 16 Brangwynne (10.1016/j.molcel.2016.05.042_bib4) 2009; 324 Brangwynne (10.1016/j.molcel.2016.05.042_bib5) 2011; 108 Banjade (10.1016/j.molcel.2016.05.042_bib1) 2014; 3 Dill (10.1016/j.molcel.2016.05.042_bib11) 2010 Kroschwald (10.1016/j.molcel.2016.05.042_bib20) 2015; 4 Nott (10.1016/j.molcel.2016.05.042_bib27) 2015; 57 Berry (10.1016/j.molcel.2016.05.042_bib3) 2015; 112 Hyman (10.1016/j.molcel.2016.05.042_bib16) 2014; 30 Burke (10.1016/j.molcel.2016.05.042_bib7) 2015; 60 Wang (10.1016/j.molcel.2016.05.042_bib33) 2014; 3 Jiang (10.1016/j.molcel.2016.05.042_bib17) 2015; 163 Fromm (10.1016/j.molcel.2016.05.042_bib13) 2014; 53 Brangwynne (10.1016/j.molcel.2016.05.042_bib6) 2015; 11 Lin (10.1016/j.molcel.2016.05.042_bib22) 2015; 60 McNaughton (10.1016/j.molcel.2016.05.042_bib23) 2009; 106 Patel (10.1016/j.molcel.2016.05.042_bib28) 2015; 162 Zhang (10.1016/j.molcel.2016.05.042_bib36) 2015; 60 Jones (10.1016/j.molcel.2016.05.042_bib18) 2006; 440 Vitalis (10.1016/j.molcel.2016.05.042_bib32) 2009; 30 Han (10.1016/j.molcel.2016.05.042_bib14) 2012; 149 |
| References_xml | – volume: 163 start-page: 108 year: 2015 end-page: 122 ident: bib17 article-title: Phase transition of spindle-associated protein regulate spindle apparatus assembly publication-title: Cell – volume: 41 start-page: D377 year: 2013 end-page: D386 ident: bib24 article-title: PANTHER in 2013: modeling the evolution of gene function, and other gene attributes, in the context of phylogenetic trees publication-title: Nucleic Acids Res. – volume: 163 start-page: 829 year: 2015 end-page: 839 ident: bib35 article-title: The LC Domain of hnRNPA2 Adopts Similar Conformations in Hydrogel Polymers, Liquid-like Droplets, and Nuclei publication-title: Cell – volume: 112 start-page: E6426 year: 2015 end-page: E6435 ident: bib2 article-title: Conserved interdomain linker promotes phase separation of the multivalent adaptor protein Nck publication-title: Proc. Natl. Acad. Sci. USA – volume: 30 start-page: 39 year: 2014 end-page: 58 ident: bib16 article-title: Liquid-liquid phase separation in biology publication-title: Annu. Rev. Cell Dev. Biol. – volume: 60 start-page: 220 year: 2015 end-page: 230 ident: bib36 article-title: RNA Controls PolyQ Protein Phase Transitions publication-title: Mol. Cell – volume: 16 start-page: 18 year: 2015 end-page: 29 ident: bib34 article-title: Intrinsically disordered proteins in cellular signalling and regulation publication-title: Nat. Rev. Mol. Cell Biol. – volume: 162 start-page: 1066 year: 2015 end-page: 1077 ident: bib28 article-title: A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation publication-title: Cell – volume: 53 start-page: 7354 year: 2014 end-page: 7359 ident: bib13 article-title: In vitro reconstitution of a cellular phase-transition process that involves the mRNA decapping machinery publication-title: Angew. Chem. Int. Ed. Engl. – volume: 112 start-page: 7189 year: 2015 end-page: 7194 ident: bib12 article-title: The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics publication-title: Proc. Natl. Acad. Sci. USA – volume: 33 start-page: 717 year: 2009 end-page: 726 ident: bib8 article-title: An architectural role for a nuclear noncoding RNA: NEAT1 RNA is essential for the structure of paraspeckles publication-title: Mol. Cell – volume: 106 start-page: 6111 year: 2009 end-page: 6116 ident: bib23 article-title: Mammalian cell penetration, siRNA transfection, and DNA transfection by supercharged proteins publication-title: Proc. Natl. Acad. Sci. USA – volume: 278 start-page: 48553 year: 2003 end-page: 48562 ident: bib25 article-title: Sequence and structure determinants for the self-aggregation of recombinant polypeptides modeled after human elastin publication-title: J. Biol. Chem. – volume: 21 start-page: 2899 year: 2012 end-page: 2911 ident: bib9 article-title: Evaluating the role of the FUS/TLS-related gene EWSR1 in amyotrophic lateral sclerosis publication-title: Hum. Mol. Genet. – volume: 324 start-page: 1729 year: 2009 end-page: 1732 ident: bib4 article-title: Germline P granules are liquid droplets that localize by controlled dissolution/condensation publication-title: Science – volume: 108 start-page: 228a year: 2015 ident: bib15 article-title: CIDER: Classification of Intrinsically Disordered Ensemble Regions publication-title: Biophys. J. – volume: 440 start-page: 818 year: 2006 end-page: 823 ident: bib18 article-title: Nck adaptor proteins link nephrin to the actin cytoskeleton of kidney podocytes publication-title: Nature – volume: 11 start-page: 899 year: 2015 end-page: 904 ident: bib6 article-title: Polymer physics of intracellular phase transitions publication-title: Nat. Phys. – volume: 149 start-page: 768 year: 2012 end-page: 779 ident: bib14 article-title: Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies publication-title: Cell – volume: 30 start-page: 673 year: 2009 end-page: 699 ident: bib32 article-title: ABSINTH: a new continuum solvation model for simulations of polypeptides in aqueous solutions publication-title: J. Comput. Chem. – volume: 57 start-page: 936 year: 2015 end-page: 947 ident: bib27 article-title: Phase transition of a disordered nuage protein generates environmentally responsive membraneless organelles publication-title: Mol. Cell – volume: 483 start-page: 336 year: 2012 end-page: 340 ident: bib21 article-title: Phase transitions in the assembly of multivalent signalling proteins publication-title: Nature – volume: 43 start-page: D315 year: 2015 end-page: D320 ident: bib29 article-title: MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins publication-title: Nucleic Acids Res. – volume: 127 start-page: 1071 year: 2006 ident: bib30 article-title: SnapShot: Cellular bodies publication-title: Cell – volume: 60 start-page: 231 year: 2015 end-page: 241 ident: bib7 article-title: Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II publication-title: Mol. Cell – volume: 149 start-page: 753 year: 2012 end-page: 767 ident: bib19 article-title: Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels publication-title: Cell – volume: 3 start-page: e04591 year: 2014 ident: bib33 article-title: Regulation of RNA granule dynamics by phosphorylation of serine-rich, intrinsically disordered proteins in C. elegans publication-title: eLife – volume: 167 start-page: 2 year: 2011 end-page: 11 ident: bib31 article-title: A review of the early development of the thermodynamics of the complex coacervation phase separation publication-title: Adv. Colloid Interface Sci. – volume: 108 start-page: 4334 year: 2011 end-page: 4339 ident: bib5 article-title: Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytes publication-title: Proc. Natl. Acad. Sci. USA – volume: 163 start-page: 123 year: 2015 end-page: 133 ident: bib26 article-title: Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization publication-title: Cell – year: 2010 ident: bib11 article-title: Molecular driving forces: statistical thermodynamics in biology, chemistry, physics, and nanoscience – volume: 60 start-page: 208 year: 2015 end-page: 219 ident: bib22 article-title: Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins publication-title: Mol. Cell – volume: 4 start-page: e06807 year: 2015 ident: bib20 article-title: Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules publication-title: eLife – volume: 3 start-page: 3 year: 2014 ident: bib1 article-title: Phase transitions of multivalent proteins can promote clustering of membrane receptors publication-title: eLife – volume: 112 start-page: E5237 year: 2015 end-page: E5245 ident: bib3 article-title: RNA transcription modulates phase transition-driven nuclear body assembly publication-title: Proc. Natl. Acad. Sci. USA – volume: 110 start-page: 13392 year: 2013 end-page: 13397 ident: bib10 article-title: Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues publication-title: Proc. Natl. Acad. Sci. USA – volume: 16 start-page: 18 year: 2015 ident: 10.1016/j.molcel.2016.05.042_bib34 article-title: Intrinsically disordered proteins in cellular signalling and regulation publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm3920 – volume: 440 start-page: 818 year: 2006 ident: 10.1016/j.molcel.2016.05.042_bib18 article-title: Nck adaptor proteins link nephrin to the actin cytoskeleton of kidney podocytes publication-title: Nature doi: 10.1038/nature04662 – volume: 43 start-page: D315 year: 2015 ident: 10.1016/j.molcel.2016.05.042_bib29 article-title: MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins publication-title: Nucleic Acids Res. doi: 10.1093/nar/gku982 – volume: 108 start-page: 4334 year: 2011 ident: 10.1016/j.molcel.2016.05.042_bib5 article-title: Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytes publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1017150108 – volume: 112 start-page: 7189 year: 2015 ident: 10.1016/j.molcel.2016.05.042_bib12 article-title: The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1504822112 – volume: 30 start-page: 673 year: 2009 ident: 10.1016/j.molcel.2016.05.042_bib32 article-title: ABSINTH: a new continuum solvation model for simulations of polypeptides in aqueous solutions publication-title: J. Comput. Chem. doi: 10.1002/jcc.21005 – volume: 163 start-page: 108 year: 2015 ident: 10.1016/j.molcel.2016.05.042_bib17 article-title: Phase transition of spindle-associated protein regulate spindle apparatus assembly publication-title: Cell doi: 10.1016/j.cell.2015.08.010 – year: 2010 ident: 10.1016/j.molcel.2016.05.042_bib11 – volume: 30 start-page: 39 year: 2014 ident: 10.1016/j.molcel.2016.05.042_bib16 article-title: Liquid-liquid phase separation in biology publication-title: Annu. Rev. Cell Dev. Biol. doi: 10.1146/annurev-cellbio-100913-013325 – volume: 163 start-page: 123 year: 2015 ident: 10.1016/j.molcel.2016.05.042_bib26 article-title: Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization publication-title: Cell doi: 10.1016/j.cell.2015.09.015 – volume: 41 start-page: D377 year: 2013 ident: 10.1016/j.molcel.2016.05.042_bib24 article-title: PANTHER in 2013: modeling the evolution of gene function, and other gene attributes, in the context of phylogenetic trees publication-title: Nucleic Acids Res. doi: 10.1093/nar/gks1118 – volume: 149 start-page: 753 year: 2012 ident: 10.1016/j.molcel.2016.05.042_bib19 article-title: Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels publication-title: Cell doi: 10.1016/j.cell.2012.04.017 – volume: 21 start-page: 2899 year: 2012 ident: 10.1016/j.molcel.2016.05.042_bib9 article-title: Evaluating the role of the FUS/TLS-related gene EWSR1 in amyotrophic lateral sclerosis publication-title: Hum. Mol. Genet. doi: 10.1093/hmg/dds116 – volume: 4 start-page: e06807 year: 2015 ident: 10.1016/j.molcel.2016.05.042_bib20 article-title: Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules publication-title: eLife doi: 10.7554/eLife.06807 – volume: 60 start-page: 208 year: 2015 ident: 10.1016/j.molcel.2016.05.042_bib22 article-title: Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins publication-title: Mol. Cell doi: 10.1016/j.molcel.2015.08.018 – volume: 53 start-page: 7354 year: 2014 ident: 10.1016/j.molcel.2016.05.042_bib13 article-title: In vitro reconstitution of a cellular phase-transition process that involves the mRNA decapping machinery publication-title: Angew. Chem. Int. Ed. Engl. doi: 10.1002/anie.201402885 – volume: 324 start-page: 1729 year: 2009 ident: 10.1016/j.molcel.2016.05.042_bib4 article-title: Germline P granules are liquid droplets that localize by controlled dissolution/condensation publication-title: Science doi: 10.1126/science.1172046 – volume: 60 start-page: 231 year: 2015 ident: 10.1016/j.molcel.2016.05.042_bib7 article-title: Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II publication-title: Mol. Cell doi: 10.1016/j.molcel.2015.09.006 – volume: 3 start-page: 3 year: 2014 ident: 10.1016/j.molcel.2016.05.042_bib1 article-title: Phase transitions of multivalent proteins can promote clustering of membrane receptors publication-title: eLife doi: 10.7554/eLife.04123 – volume: 106 start-page: 6111 year: 2009 ident: 10.1016/j.molcel.2016.05.042_bib23 article-title: Mammalian cell penetration, siRNA transfection, and DNA transfection by supercharged proteins publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.0807883106 – volume: 60 start-page: 220 year: 2015 ident: 10.1016/j.molcel.2016.05.042_bib36 article-title: RNA Controls PolyQ Protein Phase Transitions publication-title: Mol. Cell doi: 10.1016/j.molcel.2015.09.017 – volume: 108 start-page: 228a year: 2015 ident: 10.1016/j.molcel.2016.05.042_bib15 article-title: CIDER: Classification of Intrinsically Disordered Ensemble Regions publication-title: Biophys. J. doi: 10.1016/j.bpj.2014.11.1260 – volume: 483 start-page: 336 year: 2012 ident: 10.1016/j.molcel.2016.05.042_bib21 article-title: Phase transitions in the assembly of multivalent signalling proteins publication-title: Nature doi: 10.1038/nature10879 – volume: 3 start-page: e04591 year: 2014 ident: 10.1016/j.molcel.2016.05.042_bib33 article-title: Regulation of RNA granule dynamics by phosphorylation of serine-rich, intrinsically disordered proteins in C. elegans publication-title: eLife doi: 10.7554/eLife.04591 – volume: 110 start-page: 13392 year: 2013 ident: 10.1016/j.molcel.2016.05.042_bib10 article-title: Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1304749110 – volume: 112 start-page: E5237 year: 2015 ident: 10.1016/j.molcel.2016.05.042_bib3 article-title: RNA transcription modulates phase transition-driven nuclear body assembly publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1509317112 – volume: 57 start-page: 936 year: 2015 ident: 10.1016/j.molcel.2016.05.042_bib27 article-title: Phase transition of a disordered nuage protein generates environmentally responsive membraneless organelles publication-title: Mol. Cell doi: 10.1016/j.molcel.2015.01.013 – volume: 278 start-page: 48553 year: 2003 ident: 10.1016/j.molcel.2016.05.042_bib25 article-title: Sequence and structure determinants for the self-aggregation of recombinant polypeptides modeled after human elastin publication-title: J. Biol. Chem. doi: 10.1074/jbc.M308465200 – volume: 127 start-page: 1071 year: 2006 ident: 10.1016/j.molcel.2016.05.042_bib30 article-title: SnapShot: Cellular bodies publication-title: Cell doi: 10.1016/j.cell.2006.11.026 – volume: 112 start-page: E6426 year: 2015 ident: 10.1016/j.molcel.2016.05.042_bib2 article-title: Conserved interdomain linker promotes phase separation of the multivalent adaptor protein Nck publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1508778112 – volume: 11 start-page: 899 year: 2015 ident: 10.1016/j.molcel.2016.05.042_bib6 article-title: Polymer physics of intracellular phase transitions publication-title: Nat. Phys. doi: 10.1038/nphys3532 – volume: 149 start-page: 768 year: 2012 ident: 10.1016/j.molcel.2016.05.042_bib14 article-title: Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies publication-title: Cell doi: 10.1016/j.cell.2012.04.016 – volume: 162 start-page: 1066 year: 2015 ident: 10.1016/j.molcel.2016.05.042_bib28 article-title: A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation publication-title: Cell doi: 10.1016/j.cell.2015.07.047 – volume: 167 start-page: 2 year: 2011 ident: 10.1016/j.molcel.2016.05.042_bib31 article-title: A review of the early development of the thermodynamics of the complex coacervation phase separation publication-title: Adv. Colloid Interface Sci. doi: 10.1016/j.cis.2011.01.007 – volume: 163 start-page: 829 year: 2015 ident: 10.1016/j.molcel.2016.05.042_bib35 article-title: The LC Domain of hnRNPA2 Adopts Similar Conformations in Hydrogel Polymers, Liquid-like Droplets, and Nuclei publication-title: Cell doi: 10.1016/j.cell.2015.10.040 – volume: 33 start-page: 717 year: 2009 ident: 10.1016/j.molcel.2016.05.042_bib8 article-title: An architectural role for a nuclear noncoding RNA: NEAT1 RNA is essential for the structure of paraspeckles publication-title: Mol. Cell doi: 10.1016/j.molcel.2009.01.026 |
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| SubjectTerms | amino acid composition Amino Acid Sequence Animals Cell Nucleus - chemistry Cell Nucleus - metabolism Computer Simulation droplets HeLa Cells Humans Hydrophobic and Hydrophilic Interactions hydrophobicity in vitro studies Intrinsically Disordered Proteins - chemistry Intrinsically Disordered Proteins - genetics Intrinsically Disordered Proteins - metabolism Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Mice Models, Molecular mutagenesis Mutation organelles Organelles - chemistry Organelles - metabolism Protein Domains proteins Proteomics - methods separation Static Electricity Structure-Activity Relationship Surface Properties Time Factors Transfection |
| Title | Sequence Determinants of Intracellular Phase Separation by Complex Coacervation of a Disordered Protein |
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