Evidence map›Paper›PMID 30498217›Full record

ArticleNature communications2018

Compositional adaptability in NPM1-SURF6 scaffolding networks enabled by dynamic switching of phase separation mechanisms.

Mylene C Ferrolino, Diana M Mitrea, J Robert Michael, Richard W Kriwacki

Open access · goldAbstract 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 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
3.4field-weighted citation impact, top 6% 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

65 citing papers in PubMed, 118 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. METTL3/YTHDF1-Driven SURF6 Promotes Prostate Cancer Stemness via CDK4.Journal of cellular and molecular medicine · 2026
    Article
  5. Generative design of intrinsically disordered protein regions with IDiom.bioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Mechanobiology of the Nucleolus.Biology of the cell · 2026
    Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Emergent microenvironments of nucleoli.Nucleus (Austin, Tex.) · 2024
    Review
  20. p14Nature communications · 2024
    Article

5 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

4 authors at 1 institution in 1 country.

Mylene C FerrolinoDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, USA.
Diana M MitreaDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, USA.
J Robert MichaelDepartment of Computational Biology, St. Jude Children's Research Hospital, Memphis, TN, USA.
Richard W KriwackiDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, USA. richard.kriwacki@stjude.org.ORCID http://orcid.org/0000-0002-9798-6018
St. Jude Children's Research Hospital · US

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
The Molecular Basis of Liquid-like Structure of the NucleolusR01GM115634 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI KRIWACKI, RICHARD W · 2015 to 2018
$1.8M
NCI NIH HHS P30 CA021765NIGMS NIH HHS R01 GM115634
6 · The paper itself

Abstract

The nucleolus, the site for ribosome biogenesis contains hundreds of proteins and several types of RNA. The functions of many non-ribosomal nucleolar proteins are poorly understood, including Surfeit locus protein 6 (SURF6), an essential disordered protein with roles in ribosome biogenesis and cell proliferation. SURF6 co-localizes with Nucleophosmin (NPM1), a highly abundant protein that mediates the liquid-like features of the granular component region of the nucleolus through phase separation. Here, we show that electrostatically-driven interactions between disordered regions of NPM1 and SURF6 drive liquid-liquid phase separation. We demonstrate that co-existing heterotypic (NPM1-SURF6) and homotypic (NPM1-NPM1) scaffolding interactions within NPM1-SURF6 liquid-phase droplets dynamically and seamlessly interconvert in response to variations in molecular crowding and protein concentrations. We propose a mechanism wherein NPM1-dependent nucleolar scaffolds are modulated by non-ribosomal proteins through active rearrangements of interaction networks that can possibly contribute to the directionality of ribosomal biogenesis within the liquid-like nucleolus.

Indexed as

Cell NucleolusFluorescence Recovery After PhotobleachingHumansNuclear ProteinsNucleophosminOrganelle BiogenesisProtein BindingRibosomesRNA, RibosomalNPM1 protein, humanNuclear ProteinsNucleophosminRNA, RibosomalSURF6 protein, human

Identifiers

PMID30498217
PMCPMC6265330
OpenAlexW2901094661

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.