Evidence map›Paper›PMID 33798566›Full record

ArticleBiophysical journal2021

Phase separation of the LINE-1 ORF1 protein is mediated by the N-terminus and coiled-coil domain.

Jocelyn C Newton, Mandar T Naik, Grace Y Li, Eileen L Murphy, Nicolas L Fawzi, John M Sedivy, Gerwald Jogl

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

34 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
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  7. BeyondInternational journal of molecular sciences · 2025
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  16. A prion-like domain in Gag capsid protein drives retrotransposon particle assembly and mobility.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Review
  18. An interchangeable prion-like domain is required for Ty1 retrotransposition.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Article
  20. 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

7 authors at 1 institution in 1 country.

Jocelyn C NewtonDepartment of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, Rhode Island.
Mandar T NaikDepartment of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, Rhode Island.
Grace Y LiDepartment of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, Rhode Island.
Eileen L MurphyDepartment of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, Rhode Island.
Nicolas L FawziDepartment of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, Rhode Island.
John M SedivyDepartment of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, Rhode Island. Electronic address: john_sedivy@brown.edu.
Gerwald JoglDepartment of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, Rhode Island. Electronic address: gerwald_jogl@brown.edu.
Brown University · US

Funding

Somatic Activation of Retrotransposition: A New Molecular Mechanism of Aging?P01AG051449 · NIA · BROWN UNIVERSITY · PI John M Sedivy · 2016 to 2026
$30.4M
MECHANISMS OF REPLICATIVE SENESCENCE IN CELLSR01AG016694 · NIA · BROWN UNIVERSITY · PI SEDIVY, JOHN M · 1999 to 2024
$5.7M
Functional and Pathological Interactions of TDP-43R01NS116176 · NINDS · BROWN UNIVERSITY · PI FAWZI, NICOLAS LUX, MITTAL, JEETAIN · 2020 to 2024
$3.6M
NIA NIH HHS P01 AG051449NIA NIH HHS R01 AG016694NINDS NIH HHS R01 NS116176
6 · The paper itself

Abstract

Long interspersed nuclear element-1 (L1) is a retrotransposable element that autonomously replicates in the human genome, resulting in DNA damage and genomic instability. Activation of L1 in senescent cells triggers a type I interferon response and age-associated inflammation. Two open reading frames encode an ORF1 protein functioning as messenger RNA chaperone and an ORF2 protein providing catalytic activities necessary for retrotransposition. No function has been identified for the conserved, disordered N-terminal region of ORF1. Using microscopy and NMR spectroscopy, we demonstrate that ORF1 forms liquid droplets in vitro in a salt-dependent manner and that interactions between its N-terminal region and coiled-coil domain are necessary for phase separation. Mutations disrupting blocks of charged residues within the N-terminus impair phase separation, whereas some mutations within the coiled-coil domain enhance phase separation. Demixing of the L1 particle from the cytosol may provide a mechanism to protect the L1 transcript from degradation.

Indexed as

Long Interspersed Nucleotide ElementsMolecular ChaperonesHumansOpen Reading FramesProtein DomainsRNA, MessengerMolecular ChaperonesRNA, Messenger

Identifiers

PMID33798566
PMCPMC8390800
OpenAlexW3148151718

What OpenQuestion holds

Textmetadata
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.