Ultracompact Retrodirective Antenna Arrays With Superdirective Radiation Patterns

It is shown that the direction-of-arrival (DoA) information carried by an incident electromagnetic (EM) wave can be encoded into the evanescent near field of an electrically small resonance antenna array with a spatial rate higher than that of the incident field oscillation rate in free space. Phase conjugation of the received signal leads to the retrodirection of the near field in the antenna array environment, which in turn generates a retrodirected far-field beam toward the original DoA. This EM phenomenon enables electrically small retrodirective antenna arrays with superdirective, angular super-resolution, auto-pointing properties for an arbitrary DoA. A theoretical explanation of the phenomenon based on first principal observations is given and full-wave simulations demonstrate a realizability route for the proposed retrodirective terminal that is comprised of resonance dipole antenna elements. Specifically, it is shown that a three-element disk-loaded retrodirective dipole array with 0.15\lambda spacings can achieve a 3.4-dBi maximal gain, 3-dBi front-to-back ratio, and 13% return loss fractional bandwidth (at the 10-dB level). Then, it is demonstrated that the radiation gain of a three-element array can be improved to approximately 6 dBi at the expense of the return loss fractional bandwidth reduction (2%).

Actin dynamics provides membrane tension to merge fusing vesicles into the plasma membrane

Vesicle fusion is executed via formation of an Ω-shaped structure (Ω-profile), followed by closure (kiss-and-run) or merging of the Ω-profile into the plasma membrane (full fusion). Although Ω-profile closure limits release but recycles vesicles economically, Ω-profile merging facilitates release but couples to classical endocytosis for recycling. Despite its crucial role in determining exocytosis/endocytosis modes, how Ω-profile merging is mediated is poorly understood in endocrine cells and neurons containing small ∼30-300 nm vesicles. Here, using confocal and super-resolution STED imaging, force measurements, pharmacology and gene knockout, we show that dynamic assembly of filamentous actin, involving ATP hydrolysis, N-WASP and formin, mediates Ω-profile merging by providing sufficient plasma membrane tension to shrink the Ω-profile in neuroendocrine chromaffin cells containing ∼300 nm vesicles. Actin-directed compounds also induce Ω-profile accumulation at lamprey synaptic active zones, suggesting that actin may mediate Ω-profile merging at synapses. These results uncover molecular and biophysical mechanisms underlying Ω-profile merging.