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

Author

Listed:
  • Jonathon Nixon-Abell

    (University of Cambridge)

  • Francesco S. Ruggeri

    (Wageningen University & Research
    University of Cambridge)

  • Seema Qamar

    (University of Cambridge)

  • Therese W. Herling

    (University of Cambridge)

  • Magdalena A. Czekalska

    (University of Cambridge)

  • Yi Shen

    (University of Cambridge
    The University of Sydney
    The University of Sydney)

  • Guozhen Wang

    (University of Cambridge
    Zhejiang University)

  • Christopher King

    (NIH)

  • Michael S. Fernandopulle

    (University of Cambridge
    NIH
    Northwestern University)

  • Tomas Sneideris

    (University of Cambridge)

  • Joseph L. Watson

    (MRC Laboratory of Molecular Biology)

  • Visakh V. S. Pillai

    (Wageningen University & Research)

  • William Meadows

    (University of Cambridge)

  • James W. Henderson

    (University of Cambridge)

  • Joseph E. Chambers

    (University of Cambridge)

  • Jane L. Wagstaff

    (Cambridge Biomedical Campus)

  • Sioned H. Williams

    (University of Cambridge)

  • Helena Coyle

    (University of Cambridge)

  • Greta Šneiderienė

    (University of Cambridge)

  • Yuqian Lu

    (University of Cambridge)

  • Shuyuan Zhang

    (University of Cambridge)

  • Stefan J. Marciniak

    (University of Cambridge)

  • Stefan M. V. Freund

    (Cambridge Biomedical Campus)

  • Emmanuel Derivery

    (MRC Laboratory of Molecular Biology)

  • Michael E. Ward

    (NIH)

  • Michele Vendruscolo

    (University of Cambridge)

  • Tuomas P. J. Knowles

    (University of Cambridge)

  • Peter St George-Hyslop

    (University of Toronto
    Columbia University Irvine Medical Center)

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.

Suggested Citation

  • 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 & Josep, 2025. "ANXA11 biomolecular condensates facilitate protein-lipid phase coupling on lysosomal membranes," Nature Communications, Nature, vol. 16(1), pages 1-19, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-58142-5
    DOI: 10.1038/s41467-025-58142-5
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