Evidence map›Paper›PMID 40631075›Full record

ArticlebioRxiv : the preprint server for biology2025

Transient Poly(ADP-Ribose) Triggers FUS Condensation Hysteresis via a Prion-Like Mechanism.

Hongrui Liu, Yuxuan Cai, Leilei Shi, Meenakshi Pillai, Nilimesh Das, Haley E Tarbox, Yingda Ge, Kun Yue, Xingyi Yang, Piyush Rath and 8 more

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

18 authors.

Hongrui LiuDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.ORCID 0000-0002-6274-5951
Yuxuan CaiDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.
Leilei ShiDepartment of Epigenetics and Molecular Carcinogenesis, University of Texas MD Anderson Cancer Center, Houston, TX 77054, USA.ORCID 0000-0002-8895-1403
Meenakshi PillaiDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.ORCID 0009-0007-2160-4355
Nilimesh DasProgram in Cellular & Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.ORCID 0000-0003-2081-0177
Haley E TarboxDepartment of Chemistry, Johns Hopkins University, Baltimore, MD 21218, USA.ORCID 0000-0002-8672-4792
Yingda GeProgram in Cellular & Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.ORCID 0009-0007-3194-9680
Kun YueDepartment of Chemistry, Tufts University, Medford, MA 02155, USA.ORCID 0000-0002-3638-5390
Xingyi YangDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.
Piyush RathDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.ORCID 0009-0008-2974-3146
Mohsen BadieeDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.ORCID 0000-0003-3722-4609
Charina S FabilaneProgram in Molecular Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.ORCID 0000-0003-3801-7927
Jamie B SpanglerTranslational Tissue Engineering Center, School of Medicine, Johns Hopkins University, Baltimore, MD 21205, USA.ORCID 0000-0001-8187-3732
Mark T BedfordDepartment of Epigenetics and Molecular Carcinogenesis, University of Texas MD Anderson Cancer Center, Houston, TX 77054, USA.ORCID 0000-0002-8899-1050
Sua MyongProgram in Cellular & Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.ORCID 0000-0001-9098-3423
Stephen D FriedDepartment of Chemistry, Johns Hopkins University, Baltimore, MD 21218, USA.ORCID 0000-0003-2494-2193
Xinqiang DingDepartment of Chemistry, Tufts University, Medford, MA 02155, USA.ORCID 0000-0002-4598-8732
Anthony K L LeungDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.ORCID 0000-0001-5569-4036

Funding

TRAINING IN AREAS FUNDAMENTAL TO CANCER RESEARCHT32CA009110 · NCI · JOHNS HOPKINS UNIVERSITY · PI MATUNIS, MICHAEL J., WEERARATNA, ASHANI T · 1985 to 2025
$13.1M
Research Training in Age-Related Cognitive DisordersT32AG027668 · NIA · JOHNS HOPKINS UNIVERSITY · PI MARILYN S. ALBERT · 2007 to 2026
$6.3M
Role of ADP-Ribosylation in Stress Granules-Equipment SupplementR01GM104135 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Anthony K L Leung · 2015 to 2026
$4.2M
Suprachoroidal nonviral gene transfer of engineered VEGF antagonistsR01EY031097 · NEI · JOHNS HOPKINS UNIVERSITY · PI CAMPOCHIARO, PETER A, GREEN, JORDAN · 2020 to 2023
$2.4M
Molecular Assembly and Disassembly of RNA-Protein Complexes Implicated in ALS/FTDRF1NS113636 · NINDS · JOHNS HOPKINS UNIVERSITY · PI MYONG, SUA · 2019 to 2019
$2.0M
The Chemistry-Biology Interface Program at Johns Hopkins UniversityT32GM149382 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI STEVEN E ROKITA · 2023 to 2026
$1.4M
A Functional Analysis of Arginine MethylationR35GM153387 · NIGMS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI MARK T. BEDFORD · 2024 to 2026
$1.2M
Defining the Role of Poly ADP-ribose in Biomolecular Condensation in ALS and FTLDR01AG071326 · NIA · BOSTON CHILDREN'S HOSPITAL · PI LEUNG, ANTHONY K L, MYONG, SUA · 2024 to 2024
$655k
NCI NIH HHS T32 CA009110NEI NIH HHS R01 EY031097NIA NIH HHS R01 AG071326NIA NIH HHS T32 AG027668NIGMS NIH HHS R01 GM104135NIGMS NIH HHS R35 GM153387NIGMS NIH HHS T32 GM149382NINDS NIH HHS RF1 NS113636
6 · The paper itself

Abstract

Hysteresis-where a system retains memory of a transient stimulus-is common in signaling but can also arise in intracellular organization. DNA repair foci, a type of biomolecular condensate, are initiated by the short-lived noncanonical nucleic acid poly(ADP-ribose) (PAR). PAR recruits proteins with prion-like domains (PrLDs), such as Fused in Sarcoma (FUS), and initiates their condensation, which persists even after PAR degradation. How FUS transitions from PAR-dependent to PAR-independent condensation remains unclear. Here, we show that PAR binding triggers a conformational switch in FUS, enabling sustained condensation. PAR binds to the C-terminal arginine-rich region of FUS, displacing intramolecular contacts, and exposing the N-terminal PrLD. This conformational opening allows PrLD interactions

Indexed as

biomolecular condensateDNA repair fociFused in Sarcoma (FUS)Poly(ADP-ribose) (PAR)prion-like domain (PrLD)

Identifiers

PMID40631075
PMCPMC12236490

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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.