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On-Chip Octanol-Assisted Liposome Assembly for Bioengineering

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Lipidation as a post-translational code for protein liquid-liquid phase separation.

Soodabeh Abbasi Sani¹, Agnieszka Chytła¹, Martin Sztacho¹

¹Laboratory of Cancer Cell Architecture, Institute of Biochemistry and Experimental Oncology, First Faculty of Medicine, Charles University, Prague, Czech Republic.

Journal of Lipid Research

|February 15, 2026

Summary

Lipidation, the attachment of lipids to proteins, regulates biomolecular condensate formation and function. This process integrates membrane association with phase separation, influencing cellular organization and gene expression.

Keywords:

biomolecular condensates cell signaling lipid rafts membrane organization phosphoinositides phospholipids post-translational modifications transcription

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Area of Science:

Cell Biology
Biochemistry
Molecular Biology

Background:

Liquid-liquid phase separation (LLPS) drives biomolecular condensate formation, crucial for cellular organization.
Post-translational modifications like phosphorylation and ubiquitination are known to affect condensate behavior.
The role of lipidation in LLPS and condensate dynamics is less understood but critical for protein function.

Purpose of the Study:

To explore lipidation as a molecular code integrating membrane association and phase separation.
To investigate how lipidation tunes condensate assembly, composition, and function.
To propose phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) as a nuclear lipid modifier (PIPoylation) for membrane-less nuclear compartments.

Main Methods:

Review of existing literature on lipidation, LLPS, and condensate biology.
Analysis of how canonical lipidations (palmitoylation, myristoylation, prenylation, phospholipidation) impact cellular processes.
Examination of PI(4,5)P2's role in nuclear condensate structuring and its link to gene expression.

Main Results:

Lipidation dictates protein hydrophobicity and membrane affinity, influencing LLPS.
Canonical lipidations govern membrane nanodomain organization, autophagy, and nuclear condensate architecture.
PI(4,5)P2 metabolism connects chromatin remodeling and transcriptional control via LLPS.

Conclusions:

Lipidation acts as a key regulator, integrating membrane association with phase separation to control condensate properties.
PIPoylation represents a novel mechanism for structuring nuclear compartments.
Lipidation is essential for condensate-membrane communication across cellular compartments, impacting diverse biological processes.