Formation of a phase-separated interface between homologous chromosomes during meiosis enables regulatory signals to spread in cis over long distances, illuminating the longstanding mystery of crossover interference.
The transmembrane shape of the F1Fo ATP synthase monomer provides the molecular basis of high curvature at the ridges of mammalian mitochondrial cristae.
The amino acids that are necessary for phospholipid scrambling by ANO6/TMEM16F can, via domain swapping, confer scrambling activity to the chloride ion channel ANO1 that normally does not scramble phospholipids.
The SHIP2 inositol phosphatase is an important upstream regulator of the Akt signaling pathway, which requires a catalytic core formed by the phosphatase domain tightly packed to a C2 domain for its function.
The structural relationship between TMC and TMEM16 proteins provides insight into the structure and functional mechanisms of the mechanotransduction channel complex in hair cells.
The cryo-EM structure and functional characterization of the chloride-selective ion transporter Slc26a9 defines its oligomeric architecture and transport mechanism.