Evidence map›Paper›PMID 35918061›Full record

ArticleBiochemistry2022

Protein Condensate Formation via Controlled Multimerization of Intrinsically Disordered Sequences.

Mikael V Garabedian, Zhihui Su, Jorge Dabdoub, Michelle Tong, Alexander Deiters, Daniel A Hammer, Matthew C Good

Abstract read
In one paragraph

Article in Biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Interfacing bacterial microcompartment shell proteins with genetically encoded condensates.Protein science : a publication of the Protein Society · 2025
    Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
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

7 authors.

Mikael V GarabedianDepartment of Cell and Developmental Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.
Zhihui SuDepartment of Chemical and Biomolecular Engineering, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.ORCID 0000-0003-0239-5280
Jorge DabdoubDepartment of Cell and Developmental Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.
Michelle TongDepartment of Cell and Developmental Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.
Alexander DeitersDepartment of Chemistry, University of Pittsburgh, Philadelphia, Pennsylvania 15260, United States.ORCID 0000-0003-0234-9209
Daniel A HammerDepartment of Bioengineering, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.ORCID 0000-0002-3522-3154
Matthew C GoodDepartment of Cell and Developmental Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.ORCID 0000-0002-6367-1034

Funding

Programmable Synthetic Organelles Built from Disordered Proteins for Cellular EngineeringR01EB028320 · NIBIB · UNIVERSITY OF PENNSYLVANIA · PI GOOD, MATTHEW CHARLTON, HAMMER, DANIEL A · 2019 to 2022
$1.7M
NIBIB NIH HHS R01 EB028320
6 · The paper itself

Abstract

Many proteins harboring low complexity or intrinsically disordered sequences (IDRs) are capable of undergoing liquid-liquid phase separation to form mesoscale condensates that function as biochemical niches with the ability to concentrate or sequester macromolecules and regulate cellular activity. Engineered disordered proteins have been used to generate programmable synthetic membraneless organelles in cells. Phase separation is governed by the strength of interactions among polypeptides with multivalency enhancing phase separation at lower concentrations. Previously, we and others demonstrated enzymatic control of IDR valency from multivalent precursors to dissolve condensed phases. Here, we develop noncovalent strategies to multimerize an individual IDR, the RGG domain of LAF-1, using protein interaction domains to regulate condensate formation in vitro and in living cells. First, we characterize modular dimerization of RGG domains at either terminus using cognate high-affinity coiled-coil pairs to form stable condensates in vitro. Second, we demonstrate temporal control over phase separation of RGG domains fused to FRB and FKBP in the presence of dimerizer. Further, using a photocaged dimerizer, we achieve optically induced condensation both in cell-sized emulsions and within live cells. Collectively, these modular tools allow multiple strategies to promote phase separation of a common core IDR for tunable control of condensate assembly.

Indexed as

Biochemical PhenomenaIntrinsically Disordered ProteinsPhase TransitionProtein BiosynthesisProtein DomainsIntrinsically Disordered Proteins

Identifiers

PMID35918061
PMCPMC9669173

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.