Phosphoinositides play a central role in many physiological processes by assisting the recruitment of proteins to membranes through specific phosphoinositide-binding motifs. How this recruitment is coordinated in space and time is not well understood. Here we show that BIN1/M-Amphiphysin2, a protein involved in T-tubule biogenesis in muscle cells and frequently mutated in centronuclear myopathies, clusters PtdIns(4,5)P₂ to recruit its downstream partner dynamin. By using several mutants associated with centronuclear myopathies, we find that the N-BAR and the SH3 domains of BIN1 control the kinetics and the accumulation of dynamin on membranes, respectively. We show that phosphoinositide clustering is a mechanism shared by other proteins that interact with PtdIns(4,5)P₂, but do not contain a BAR domain. Our numerical simulations point out that clustering is a diffusion-driven process in which phosphoinositide molecules are not sequestered. We propose that this mechanism plays a key role in the recruitment of downstream phosphoinositide-binding proteins.

Fabricating Quartz: Quartz is used industrially as an abrasive, as an inert glassy material, or for high-quality crystals in microelectronics. It is also valued for its piezoelectronic properties. However, it is hard to grow quartz as a patterned material or to integrate it into nanostructured devices. Carretero-Genevrier et al. (p. 827 ; see the Perspective by Brinker and Clem ) have developed a method for preparing oriented epitaxial thin films of polycrystalline α-quartz on single-crystal silicon substrates using ambient pressure and temperatures below 1000°C. Different processing conditions can be used to fabricate quartz films with a variety of pore sizes or as a dense nonporous α-quartz film.