The skyrmion, a vortex-like spin-swirling object, is anticipated to play a vital role in quantum magneto-transport processes such as the quantum Hall and topological Hall effects. The existence of the magnetic skyrmion crystal (SkX) state was recently verified experimentally for MnSi and Fe(0.5)Co(0.5)Si by means of small-angle neutron scattering and Lorentz transmission electron microscopy. However, to enable the application of such a SkX for spintronic function, materials problems such as a low crystallization temperature and low stability of SkX have to be overcome. Here we report the formation of SkX close to room temperature in thin-films of the helimagnet FeGe. In addition to the magnetic twin structure, we found a magnetic chirality inversion of the SkX across lattice twin boundaries. Furthermore, for thin crystal plates with thicknesses much smaller than the SkX lattice constant (as) the two-dimensional SkX is quite stable over a wide range of temperatures and magnetic fields, whereas for quasi-three-dimensional films with thicknesses over as the SkX is relatively unstable and observed only around the helical transition temperature. The room-temperature stable SkX state as promised by this study will pave a new path to designing quantum-effect devices based on the controllable skyrmion dynamics.

Motile cilia induce fluid movement through their rhythmic beating activity. In mammals, the transcription factor Foxj1 has been implicated in motile cilia formation. Here we show that a zebrafish Foxj1 homolog, foxj1a, is a target of Hedgehog signaling in the floor plate. Loss of Foxj1a compromises the assembly of motile cilia that decorate floor plate cells. Besides the floor plate, foxj1a is expressed in Kupffer's vesicle and pronephric ducts, where it also promotes ciliary differentiation. We show that Foxj1a activates a constellation of genes essential for motile cilia formation and function, and that its activity is sufficient for ectopic development of cilia that resemble motile cilia. We also document that a paralogous gene, foxj1b, is expressed in the otic vesicle and seems to regulate motile cilia formation in this tissue. Our findings identify a dedicated master regulatory role for Foxj1 in the transcriptional program that controls the production of motile cilia.

Magnetotransport properties have been investigated for epitaxial thin films of B20-type MnSi grown on Si(111) substrates. Lorentz transmission electron microscopy images clearly point to the robust formation of Skyrmions over a wide temperature-magnetic field region. New features distinct from those reported previously for MnSi are observed for epitaxial films: a shorter (nearly half) period of the spin helix and Skyrmions, and a topological Hall effect anomaly consisting in ∼2.2 times enhancement of the amplitude and in the opposite sign with respect to bulk samples.

The serine/threonine kinase Prk1p is known to be involved in the regulation of the actin cytoskeleton organization in budding yeast. One possible function of Prk1p is the negative regulation of Pan1p, an actin patch regulatory protein that forms a complex in vivo with at least two other proteins, Sla1p and End3p. In this report, we identified Sla1p as another substrate for Prk1p. The phosphorylation of Sla1p by Prk1p was established in vitro with the use of immunoprecipitated Prk1p and in vivo with the use of PRK1 overexpression, and was further supported by the finding that immunoprecipitated Sla1p contained PRK1-and ARK1-dependent kinase activities. Stable complex formation between Prk1p and Sla1p/Pan1p in vivo could be observed once the phosphorylation reaction was blocked by mutation in the catalytic site of Prk1p. Elevation of Prk1p activities in wild-type cells resulted in a number of deficiencies, including those in colocalization of Pan1p and Sla1p, endocytosis, and cell wall morphogenesis, likely attributable to a disintegration of the Pan1p/Sla1p/End3p complex. These results lend a strong support to the model that the phosphorylation of the Pan1p/Sla1p/End3p complex by Prk1p is one of the important mechanisms by which the organization and functions of the actin cytoskeleton are regulated.