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.
FERONIA receptor kinase interacts with phosphatidylinositol-anchored proteins LORELEI and LLG1 to ensure its proper functional location in the cell membrane and engages them as co-receptors on the cell surface to mediate a broad spectrum of growth and signaling processes.
Detailed structural analysis of NPAS1-ARNT and NPAS3-ARNT complexes, and further comparisons with other bHLH-PAS protein structures, show that this family of mammalian transcription factors have distinct ligand-binding pockets within their molecular architectures.
A domain-general structure learning mechanism, supported by anterior insula, moves beyond explicit category labels and dyadic similarity as the sole inputs to social group representations and predicts ally-choice behavior.
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.