Protein recruitment through indirect mechanochemical interactions

Abstract

Some of the key proteins essential for important cellular processes are capable of recruiting other proteins from the cytosol to phospholipid membranes. The physical basis for this cooperativity of binding is, surprisingly, still unclear. Here, we suggest a general feedback mechanism that explains cooperativity through mechanochemical coupling mediated by the mechanical properties of phospholipid membranes. Our theory predicts that protein recruitment, and therefore also protein pattern formation, involves membrane deformation, and is strongly affected by membrane composition.

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Cited by in corpus (5)

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• Controlling Uncertainty of Empirical First-Passage Times in the Small-Sample Regime
• Geometry-induced patterns through mechanochemical coupling
• Self-organisation of Protein Patterns
• Coupling between Phase Separation and Geometry on a Closed Elastic Curve: Free Energy Minimization and Dynamics