Evidence map›Paper›PMID 30061688›Full record

ArticleNature communications2018

Controllable protein phase separation and modular recruitment to form responsive membraneless organelles.

Benjamin S Schuster, Ellen H Reed, Ranganath Parthasarathy, Craig N Jahnke, Reese M Caldwell, Jessica G Bermudez, Holly Ramage, Matthew C Good, Daniel A Hammer

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 198 papers.

0numbers the graph read from it
0cells of the map it votes in
198citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

198 citing papers in PubMed.

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  15. Programmable artificial RNA condensates in mammalian cells.bioRxiv : the preprint server for biology · 2026
    Article
  16. Article
  17. Article
  18. Review
  19. Engineered membraneless organelles inSynthetic and systems biotechnology · 2025
    Article
  20. Article

138 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Benjamin S SchusterDepartment of Bioengineering, University of Pennsylvania, 210 S. 33rd St, Philadelphia, PA, 19104, USA.ORCID http://orcid.org/0000-0002-6468-8081
Ellen H ReedDepartment of Chemical and Biomolecular Engineering, University of Pennsylvania, 220 S. 33rd St., Philadelphia, PA, 19104, USA.
Ranganath ParthasarathyDepartment of Bioengineering, University of Pennsylvania, 210 S. 33rd St, Philadelphia, PA, 19104, USA.
Craig N JahnkeDepartment of Chemical and Biomolecular Engineering, University of Pennsylvania, 220 S. 33rd St., Philadelphia, PA, 19104, USA.
Reese M CaldwellDepartment of Cell and Developmental Biology, University of Pennsylvania, 421 Curie Blvd., Philadelphia, PA, 19104, USA.
Jessica G BermudezDepartment of Bioengineering, University of Pennsylvania, 210 S. 33rd St, Philadelphia, PA, 19104, USA.ORCID http://orcid.org/0000-0001-8622-677X
Holly RamageDepartment of Microbiology, University of Pennsylvania, 3610 Hamilton Walk, Philadelphia, PA, 19104, USA.
Matthew C GoodDepartment of Bioengineering, University of Pennsylvania, 210 S. 33rd St, Philadelphia, PA, 19104, USA. mattgood@pennmedicine.upenn.edu.
Daniel A HammerDepartment of Bioengineering, University of Pennsylvania, 210 S. 33rd St, Philadelphia, PA, 19104, USA. hammer@seas.upenn.edu.ORCID http://orcid.org/0000-0002-3522-3154

Funding

TRAINING PROGRAM IN CELL AND MOLECULAR BIOLOGYT32GM007229 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI BARTOLOMEI, MARISA S. · 1985 to 2023
$14.0M
Engineering protein vesicles for drug delivery applicationsF32GM119430 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI SCHUSTER, BENJAMIN S · 2016 to 2018
$142k
NIGMS NIH HHS F32 GM119430NIGMS NIH HHS T32 GM007229U.S. Department of Energy (DOE) DE-SC0007063U.S. Department of Health & Human Services | National Institutes of Health (NIH) F32GM119430
6 · The paper itself

Abstract

Many intrinsically disordered proteins self-assemble into liquid droplets that function as membraneless organelles. Because of their biological importance and ability to colocalize molecules at high concentrations, these protein compartments represent a compelling target for bio-inspired materials engineering. Here we manipulated the intrinsically disordered, arginine/glycine-rich RGG domain from the P granule protein LAF-1 to generate synthetic membraneless organelles with controllable phase separation and cargo recruitment. First, we demonstrate enzymatically triggered droplet assembly and disassembly, whereby miscibility and RGG domain valency are tuned by protease activity. Second, we control droplet composition by selectively recruiting cargo molecules via protein interaction motifs. We then demonstrate protease-triggered controlled release of cargo. Droplet assembly and cargo recruitment are robust, occurring in cytoplasmic extracts and in living mammalian cells. This versatile system, which generates dynamic membraneless organelles with programmable phase behavior and composition, has important applications for compartmentalizing collections of proteins in engineered cells and protocells.

Indexed as

Amino Acid MotifsAnimalsCaenorhabditis elegansCell Line, TumorCloning, MolecularCytoplasmCytoplasmic GranulesGene Expression Regulation, DevelopmentalHEK293 CellsHeLa CellsHumansIntrinsically Disordered ProteinsOrganellesOxidation-ReductionPermeabilityProtein DomainsIntrinsically Disordered ProteinsRecombinant Proteins

Identifiers

PMID30061688
PMCPMC6065366

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.