Evidence map›Paper›PMID 37586369›Full record

ArticleCell reports2023

An evolutionarily nascent architecture underlying the formation and emergence of biomolecular condensates.

Nima Jaberi-Lashkari, Byron Lee, Fardin Aryan, Eliezer Calo

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
4.6field-weighted citation impact, top 5% of its field
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

16 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. Nucleolar Dynamics During Oogenesis.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Emergent microenvironments of nucleoli.Nucleus (Austin, Tex.) · 2024
    Review
  15. Article
  16. 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

4 authors at 1 institution in 1 country.

Nima Jaberi-LashkariDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Byron LeeDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Fardin AryanDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Eliezer CaloDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA; David H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. Electronic address: calo@mit.edu.
Massachusetts Institute of Technology · US

Funding

VIRUS PRODUCTION COREP30CA014051 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI Jacqueline A. Lees · 1985 to 2026
$93.9M
PRE-DOCTORAL TRAINING IN THE BIOLOGICAL SCIENCEST32GM007287 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BELL, STEPHEN P., KEATING, AMY E · 1985 to 2019
$40.8M
Mechanisms regulating ribosome assembly and function in stem cells and vertebrate development.R35GM142634 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI Eliezer Calo-Velazquez · 2021 to 2026
$2.3M
NCI NIH HHS P30 CA014051NIGMS NIH HHS R35 GM142634NIGMS NIH HHS T32 GM007287
6 · The paper itself

Abstract

Biomolecular condensates are implicated in core cellular processes such as gene regulation and ribosome biogenesis. Although the architecture of biomolecular condensates is thought to rely on collective interactions between many components, it is unclear how the collective interactions required for their formation emerge during evolution. Here, we show that the structure and evolution of a recently emerged biomolecular condensate, the nucleolar fibrillar center (FC), is explained by a single self-assembling scaffold, TCOF1. TCOF1 is necessary to form the FC, and it structurally defines the FC through self-assembly mediated by homotypic interactions of serine/glutamate-rich low-complexity regions (LCRs). Finally, introduction of TCOF1 into a species lacking the FC is sufficient to form an FC-like biomolecular condensate. By demonstrating that a recently emerged biomolecular condensate is built on a simple architecture determined by a single self-assembling protein, our work provides a compelling mechanism by which biomolecular condensates can emerge in the tree of life.

Indexed as

Biomolecular CondensatesCell NucleolusGlutamic AcidProtein DomainsSerineGlutamic AcidSerinebiophysicscondensatesCP: Cell biologyCP: Molecular biologyevolutionlow-complexity regionsnucleolusphase separationscaffoldsself-assembly

Identifiers

PMID37586369
PMCPMC10529244
OpenAlexW4385841469

What Socratic holds

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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 Socratic graph.