Volume 17 Issue 8, August 2016

The proliferation marker Ki67 acts like a biological surfactant to keep mitotic chromosomes separate in the cytoplasm.

Hrd1 may form a channel regulated by autoubiquitylation that has a major role in translocating misfolded proteins from the ER lumen to the cytoplasm for subsequent degradation.

Proteins of the mitotic checkpoint regulate insulin receptor internalization through clathrin-mediated endocytosis, thereby modulating insulin signalling and systemic glucose metabolism.

It turns out that Meselson and Stahl were not the first to show that DNA replicates semi-conservatively. The preceding experiment was almost forgotten, partly because it showed something incredible.

The endonuclease CPS-6 mediates the degradation of paternal mitochondrial DNA and promotes paternal mitochondrial elimination through autophagy inCaenorhabditis elegans.

Recent structural, biochemical and single-molecule biophysical studies have elucidated the molecular mechanisms underlying the control of SNARE (solubleN-ethylmaleimide-sensitive factor attachment protein receptor) complex assembly and disassembly by chaperones.

Embryonic, brown adipocytes, together with beige, brown-like adipocytes induced in white fat depots in response to various stimuli, constitute specialized heat-producing fat cells that contribute to organismal energy expenditure. Important insights have now been gained into the transcriptional and epigenetic regulation of biogenesis and thermogenesis of these cells, opening up new possibilities for the treatment of metabolic disorders.

Rho GTPases, which cycle between a GTP-bound active form and a GDP-bound inactive form, regulate cytoskeletal and cell adhesion dynamics and thus are crucial for the coordination of cell migration, cell polarity and cell cycle progression. Rho GTPases and their regulators (GEFs, GAPs and GDIs) are also regulated by post-translational modifications and the formation of regulatory complexes to ensure precise spatiotemporal Rho GTPase activation.

When animal cells divide, they undergo dramatic changes in shape, polarity and mechanical properties. At mitotic entry, the remodelling of cortical actomyosin and cell–substrate adhesions, combined with osmotic swelling enable cell rounding, which is then reversed as cells exit mitosis. We now have a better understanding of the regulation of such shape changes and how they contribute to accurate segregation of chromosomes and other cellular components.

Many proteins that canonically function in the cytosol can also localize to the nucleus. The authors propose that a distinct group of such proteins (which they name STRaNDs) engage in a particular mode of signal transduction, whereby in response to extracellular cues, the cytosolic protein transits to the nucleus and regulates gene expression without direct DNA binding.