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, Joseph L. Watson, Visakh V. S. Pillai, William Meadows, James W. Henderson, Joseph E. Chambers, Jane L. Wagstaff, Sioned H. Williams, Helena Coyle, Greta Šneiderienė, Yuqian Lu, Shuyuan Zhang, Stefan J. Marciniak, Stefan M. V. Freund, Emmanuel Derivery, Michael E. Ward, Michele Vendruscolo, Tuomas P. J. Knowles and Peter St George-Hyslop ()
Additional contact information
Jonathon Nixon-Abell: University of Cambridge
Francesco S. Ruggeri: Wageningen University & Research
Seema Qamar: University of Cambridge
Therese W. Herling: University of Cambridge
Magdalena A. Czekalska: University of Cambridge
Yi Shen: University of Cambridge
Guozhen Wang: University of Cambridge
Christopher King: NIH
Michael S. Fernandopulle: University of Cambridge
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

Nature Communications, 2025, vol. 16, issue 1, 1-19

Abstract: 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.

Date: 2025
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DOI: 10.1038/s41467-025-58142-5

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