The structure of the yeast RSC complex, a member of the SWI/SNF chromatin remodeling family, determined by cryo-electron microscopy, reveals a conserved structural core and the mode of nucleosome engagement.

A combination of genetics, expression, genomic localization, and genomic nucleosome profiling demonstrates antagonism between two chromatin remodelers that reveal different mechanisms at different promoter architectures.

A SWI/SNF-family chromatin remodeling subcomplex from yeast is identified (RSC1) that is specialized to slide nucleosomes residing on DNA sequences that confer partial nucleosome unwrapping, with assistance from accessory factors.

Asc1/RACK1 promotes the translation of mRNAs associated with the translational closed loop complex, which have short open reading frames and encode proteins required for core metabolic processes.

A combination of genetic, electrophysiological, and modeling approaches reveals that presynaptic Rac1 is a key molecule that controls synaptic strength and plasticity by regulating the synaptic vesicle cycle steps controlling the number of fusion competent synaptic vesicles.

Multiple mechanisms, by which a highly conserved chromatin-remodeling factor RSC facilitates initiation and maintenance of large-scale, rapid gene expression upon exit from quiescent state, have been discovered.

Transcriptomic and genetic analyses of FoxO target genes reveal a key function of ER-associated protein degradation in growth regulation of Tsc1-deficient tissues.

Structural, biochemical, and cell biology study revealed that Rsu1, through binding to PINCH1, inhibits the actin bundling ability of ILK/PINCH/Parvin to regulate the actin dynamics at focal adhesion.

Presynaptic Rac1 inhibition in the hippocampus impairs spatial working memory, potentially by modulating the synaptic cytoskeleton and kinase-mediated phosphorylation of key synaptic vesicle proteins.

The GLS2 enzyme suppresses cancer metastasis by interacting with the small GTPase Rac1 and inhibiting its activity.