The LINC complex has a core 6:6 structure in which KASH-binding induces head-to-head interactions between SUN trimers, suggesting force transduction between cytoskeletal and nuclear components through branched LINC complex networks.
Repression of gene expression by the histone methyltransferase G9a is guided by two zinc finger proteins that can recognize consensus sequences in DNA.
Synaptic zinc is a novel modulator of cortical sound processing - a modulator that increases the gain of principal neurons, but reduces the gain of interneurons.
In humans, specific sequence features can predict whether meiotic recombination occurs at sites bound by the protein PRDM9, whose DNA-binding zinc-finger domain can unexpectedly bind to gene promoters and to other copies of PRDM9.
Forces stemming from cell-matrix adhesions, but not cell-cell adhesions, are directly transmitted to the nuclear lamina to regulate epidermal cell fate.
p53 folding is critically dependent on zinc, and a synthetic metallochaperone rescues tumorigenic mutations that reduce p53's zinc affinity as well as thermodynamic stability.
Unbiased ChIP-seq screens and genetic knockouts of large Kruppel associated box zinc finger protein (KRAB-ZFP) clusters reveal that evolutionarily young KRAB-ZFPs play a redundant role in retrotransposon restriction in mice.
The LINC complex, that couples the interphase cytoskeleton to the nucleus, regulates the processing of a cluster of miRNAs required for muscle regeneration by recruiting and interacting directly with Drosha.
Phosphate accumulation in zinc-deficient Arabidobsis shoots is regulated by a pathway involving the transcription factor bZIP23, the phospholipid-remodelling enzyme LPCAT1 and the transporter PHT1;1.
