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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.

ULK3 is a kinase in the abscission checkpoint that temporarily inactivates ESCRT-III proteins via phosphorylation, which is required to delay cytokinesis in response to defects in mitosis.

Cohesin loading at centromeres depends on a conserved surface cluster of amino-acid residues on the cohesin loading protein, Scc4.

The structure of the Ana2 Central Coiled-Coil Domain provides insight into how centriolar cartwheel components may be recruited and assembled, and indicates that cartwheel assembly involves more than just SAS-6 oligomerisation.

SAS-5 forms oligomers, through a trimeric coiled coil and novel dimeric domain, that are necessary for centriolar localisation of SAS-5 and for centriole duplication.

The localization of respiratory complexes in the cell membrane emerges as a critical factor for controlling respiration in bacteria.

The ability of cells to transmit information encoded in signaling dynamics is fundamentally limited by the gene decoding step.

A new family of sterol-specific lipid transfer proteins has been found that anchors in the endoplasmic reticulum; some of these proteins stretch across membrane contacts and mediate sterol traffic from the plasma membrane.

An endosomal component employs a novel PAM2-like motif to recruit a key RNA-binding protein, which explains how mRNAs and associated ribosomes are attached to endosomes during coupled transport.

The ATM kinase has an unanticipated role in tumor progression through the regulation of cell migration by oxidative stress.