Evidence map›Paper›PMID 33918018›Full record

ArticleCells2021

The F-Actin-Binding MPRIP Forms Phase-Separated Condensates and Associates with PI(4,5)P2 and Active RNA Polymerase II in the Cell Nucleus.

Can Balaban, Martin Sztacho, Michaela Blažíková, Pavel Hozák

Open access · goldAbstract read
In one paragraph

Article in Cells, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Recent advances in nuclear actin research.Nucleus (Austin, Tex.) · 2025
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. SF-1 Induces Nuclear PIP2.Biomolecules · 2023
    Article
  10. Myosin in chromosome organisation and gene expression.Biochemical Society transactions · 2023
    Review
  11. Article
  12. Med25 Limits Master Regulators That Govern Adipogenesis.International journal of molecular sciences · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
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.

Can BalabanDepartment of Biology of the Cell Nucleus, Institute of Molecular Genetics of the Czech Academy of Sciences, v.v.i., 142 20 Prague, Czech Republic.
Martin SztachoDepartment of Biology of the Cell Nucleus, Institute of Molecular Genetics of the Czech Academy of Sciences, v.v.i., 142 20 Prague, Czech Republic.
Michaela BlažíkováLight Microscopy Core Facility, Institute of Molecular Genetics of the Czech Academy of Sciences, v.v.i., 142 20 Prague, Czech Republic.ORCID 0000-0003-1227-0393
Pavel HozákDepartment of Biology of the Cell Nucleus, Institute of Molecular Genetics of the Czech Academy of Sciences, v.v.i., 142 20 Prague, Czech Republic.ORCID 0000-0003-1901-1394
Czech Academy of Sciences, Institute of Molecular Genetics · CZ

Funding

Czech Academy of Sciences JSPS 20 06EuroCellNet COST Action CA15214European Regional Development Fund CZ.1.05/1.1.00/02.0109European Regional Development Fund Project CZ.02.1.01/0.0/0.0/16_013/0001775Grantová Agentura České Republiky 19 05608S, 18 19714SInstitute of Molecular Genetics of the Czech Academy of Sciences RVO: 68378050Ministry of Education, Youth and Sports of Czech Republic COST Inter excellence internship LTC19048, LTC20024Ministry of Education, Youth and Sports of Czech Republic - Czech BioImaging LM2018129
6 · The paper itself

Abstract

Here, we provide evidence for the presence of Myosin phosphatase rho-interacting protein (MPRIP), an F-actin-binding protein, in the cell nucleus. The MPRIP protein binds to Phosphatidylinositol 4,5-bisphosphate (PIP2) and localizes to the nuclear speckles and nuclear lipid islets which are known to be involved in transcription. We identified MPRIP as a component of RNA Polymerase II/Nuclear Myosin 1 complex and showed that MPRIP forms phase-separated condensates which are able to bind nuclear F-actin fibers. Notably, the fibrous MPRIP preserves its liquid-like properties and reforms the spherical shaped condensates when F-actin is disassembled. Moreover, we show that the phase separation of MPRIP is driven by its long intrinsically disordered region at the C-terminus. We propose that the PIP2/MPRIP association might contribute to the regulation of RNAPII transcription via phase separation and nuclear actin polymerization.

Indexed as

ActinsAdaptor Proteins, Signal TransducingCell Line, TumorCell NucleusGlycolsGreen Fluorescent ProteinsHumansMyosin Type IPhosphatidylinositol 4,5-DiphosphateProtein BindingProtein DomainsRNA Polymerase IISubcellular FractionsActinsAdaptor Proteins, Signal TransducingGlycolsGreen Fluorescent Proteinshexamethylene glycolMPRIP protein, humanMYO1C protein, humanMyosin Type IPhosphatidylinositol 4,5-DiphosphateRNA Polymerase IIactinMPRIPnucleusphase separationPIP2

Identifiers

PMID33918018
PMCPMC8068864
OpenAlexW3155406114

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.