Evidence map›Paper›PMID 40118863›Full record

ArticleNature communications2025

ANXA11 biomolecular condensates facilitate protein-lipid phase coupling on lysosomal membranes.

Jonathon Nixon-Abell, Francesco S Ruggeri, Seema Qamar, Therese W Herling, Magdalena A Czekalska, Yi Shen, Guozhen Wang, Christopher King, Michael S Fernandopulle, Tomas Sneideris and 18 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2025. 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
–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

16 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Biomolecular Condensates Dictate the Folding Landscape of Proteins.bioRxiv : the preprint server for biology · 2026
    Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. Review
  14. Revisiting the role of Annexins in membrane trafficking.Cellular and molecular life sciences : CMLS · 2025
    Review
  15. Article
  16. The structural properties of full-length annexin A11.Frontiers in molecular biosciences · 2024
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

28 authors.

Jonathon Nixon-AbellDepartment of Clinical Neurosciences, Cambridge Institute for Medical Research, Clinical School, University of Cambridge, Cambridge, UK. jjn36@cam.ac.uk.ORCID http://orcid.org/0000-0003-4169-0012
Francesco S RuggeriPhysical Chemistry and Soft matter, Wageningen University & Research, Stippeneng, The Netherlands.ORCID http://orcid.org/0000-0002-1232-1907
Seema QamarDepartment of Clinical Neurosciences, Cambridge Institute for Medical Research, Clinical School, University of Cambridge, Cambridge, UK.
Therese W HerlingYusuf Hamied Department of Chemistry, Centre for Misfolding Diseases, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-1332-3090
Magdalena A CzekalskaYusuf Hamied Department of Chemistry, Centre for Misfolding Diseases, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-4494-4463
Yi ShenYusuf Hamied Department of Chemistry, Centre for Misfolding Diseases, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-0456-3850
Guozhen WangDepartment of Clinical Neurosciences, Cambridge Institute for Medical Research, Clinical School, University of Cambridge, Cambridge, UK.
Christopher KingNational institute for Neurological Disorder and Stroke, NIH, Bethesda, MD, USA.
Michael S FernandopulleDepartment of Clinical Neurosciences, Cambridge Institute for Medical Research, Clinical School, University of Cambridge, Cambridge, UK.
Tomas SneiderisYusuf Hamied Department of Chemistry, Centre for Misfolding Diseases, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0001-5285-871X
Joseph L WatsonCell Biology Division, MRC Laboratory of Molecular Biology, Cambridge, UK.ORCID http://orcid.org/0000-0001-5492-0249
Visakh V S PillaiPhysical Chemistry and Soft matter, Wageningen University & Research, Stippeneng, The Netherlands.ORCID http://orcid.org/0000-0003-1870-4391
William MeadowsDepartment of Clinical Neurosciences, Cambridge Institute for Medical Research, Clinical School, University of Cambridge, Cambridge, UK.
James W HendersonDepartment of Clinical Neurosciences, Cambridge Institute for Medical Research, Clinical School, University of Cambridge, Cambridge, UK.
Joseph E ChambersDepartment of Clinical Neurosciences, Cambridge Institute for Medical Research, Clinical School, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0003-4675-0053
Jane L WagstaffStructure Studies Division, NMR Facility, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge, UK.
Sioned H WilliamsDepartment of Clinical Neurosciences, Cambridge Institute for Medical Research, Clinical School, University of Cambridge, Cambridge, UK.
Helena CoyleDepartment of Clinical Neurosciences, Cambridge Institute for Medical Research, Clinical School, University of Cambridge, Cambridge, UK.
Greta ŠneiderienėYusuf Hamied Department of Chemistry, Centre for Misfolding Diseases, University of Cambridge, Cambridge, UK.
Yuqian LuYusuf Hamied Department of Chemistry, Centre for Misfolding Diseases, University of Cambridge, Cambridge, UK.
Shuyuan ZhangYusuf Hamied Department of Chemistry, Centre for Misfolding Diseases, University of Cambridge, Cambridge, UK.
Stefan J MarciniakDepartment of Clinical Neurosciences, Cambridge Institute for Medical Research, Clinical School, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0001-8472-7183
Stefan M V FreundStructure Studies Division, NMR Facility, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge, UK.ORCID http://orcid.org/0000-0002-7031-9872
Emmanuel DeriveryCell Biology Division, MRC Laboratory of Molecular Biology, Cambridge, UK.ORCID http://orcid.org/0000-0003-3927-5944
Michael E WardNational institute for Neurological Disorder and Stroke, NIH, Bethesda, MD, USA.ORCID http://orcid.org/0000-0002-5296-8051
Michele VendruscoloYusuf Hamied Department of Chemistry, Centre for Misfolding Diseases, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-3616-1610
Tuomas P J KnowlesYusuf Hamied Department of Chemistry, Centre for Misfolding Diseases, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-7879-0140
Peter St George-HyslopDepartment of Medicine (Division of Neurology), Temerty Faculty of Medicine, University Health Network, University of Toronto, Toronto, ON, Canada. ps2764@cumc.columbia.edu.ORCID http://orcid.org/0000-0003-0796-7209

Funding

Mechanisms of autophagic dysfunction in progranulin-related neurodegenerationF30AG060722 · NIA · NORTHWESTERN UNIVERSITY AT CHICAGO · PI FERNANDOPULLE, MICHAEL · 2018 to 2022
$203k
NIA NIH HHS F30 AG060722Wellcome Trust FC001029
6 · The paper itself

Abstract

Phase transitions of cellular proteins and lipids play a key role in governing the organisation and coordination of intracellular biology. Recent work has raised the intriguing prospect that phase transitions in proteins and lipids can be co-regulated. Here we investigate this possibility in the ribonucleoprotein (RNP) granule-ANXA11-lysosome ensemble, where ANXA11 tethers RNP granules to lysosomal membranes to enable their co-trafficking. We show that changes to the protein phase state within this system, driven by the low complexity ANXA11 N-terminus, induces a coupled phase state change in the lipids of the underlying membrane. We identify the ANXA11 interacting proteins ALG2 and CALC as potent regulators of ANXA11-based phase coupling and demonstrate their influence on the nanomechanical properties of the ANXA11-lysosome ensemble and its capacity to engage RNP granules. The phenomenon of protein-lipid phase coupling we observe within this system serves as a potential regulatory mechanism in RNA trafficking and offers an important template to understand other examples across the cell whereby biomolecular condensates closely juxtapose organellar membranes.

Indexed as

Biomolecular CondensatesIntracellular MembranesLysosomesAnimalsHeLa CellsHumansPhase TransitionRibonucleoproteinsRibonucleoproteins

Identifiers

PMID40118863
PMCPMC11928461

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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.