Résumé
Tubular lipid membranes (TLMs) are nanoscopic cylindrical assemblies that play a fundamental role in many intracellular and intercellular processes like protein trafficking, signaling and organelle morphogenesis. TLMs are generated by different mechanochemical actions, ranging from mechanical forces produced by motor proteins pulling at one TLM-end up to specific chemical activities of membrane-associated proteins. We develop here a theory of a resonant effect in protein-membrane coupling taking place in the vicinity of instabilities in tubular lipid membranes (TLMs) under longitudinal force and pressure difference constraints. Two critical low-energy modes defining the stability domain boundaries are found. We show that these modes mediate long-range TLM-protein coupling and interactions between absorbed proteins. Besides, TLM mechanical instabilities strongly influence protein desorption and protein cluster nucleation on TLMs. Experiments involving nanomechanical devices extracting TLM over a large spectrum of mechanochemical conditions can directly test model predictions.