Abstract
The typical cell contains ca. 25 vol.-% protein, of which ca. 10% forms cytoskeletal filaments and ca. 90% is non-aggregating globular protein [1]. It has previously been theoretically predicted that, under such highly crowded conditions, rigid filaments will coalesce into tight bundles coexisting with an isotropic solution of globular proteins [2]. In the present work we show that such spontaneous bundling will occur even when filament flexibility is taken into account because the persistence length of the filaments is much longer than the diameter of the globular proteins. The theoretical results are consistent with experimentally observed bundling of F-actin (the most flexible of the three most common types of cytoskeletal filaments) in the presence of globular macromolecules [3,4]. The main effect of increased filament flexibility on bundling is to cause somewhat looser packing. In mixtures of filaments, differences in flexibilities can lead to segregation. This segregation is accentuated when the stiffer filament is also wider. The results suggest that actin filaments and microtubules will spontaneously form segregated bundles in the presence of cellular concentrations of globular proteins. While cross-linking proteins may serve to stabilize these bundles, their more important function in bundling may be to fine tune the structure (e.g., polarity and registration of filaments).