Our cycle of sleep and wakefulness is controlled by a daily (circadian) body clock in our brain. When this cycle happens in a regular way people function well, but when this cycle is disturbed it can lead to a severely disrupted life. The suprachiasmatic nucleus (SCN) is part of the body clock and individual neurons of the SCN contain their own 24-hour clock, but they operate best when connected together in their neural circuit and run in synchrony.
New research, from a team of scientists in the LMB’s Structural Studies Division and the Texas A&M Health Science Center, illustrates the molecular mechanism behind a fundamental cellular process.
The research, published in PNAS, provides new insights into the way in which components of the nuclear protein transport machinery move through nuclear pores. Nuclear pores are large protein complexes that cross the nuclear envelope – the double membrane surrounding the eukaryotic cell nucleus.
New research, led by Leo James and Will McEwan from the LMB’s PNAC Division, has uncovered a previously unrecognised mechanism of intracellular pathogen detection which may provide a deeper understanding of how antibodies help fight disease and lead to the design of better vaccines and gene therapies.
Earlier research from Leo’s group showed that viruses carry antibodies into cells when they infect them .
G-protein-coupled receptors (GPCRs) are a family of cell-surface proteins that are vital for various physiological functions including vision, smell, taste, and behavior. They are also the pharmacological targets of ~30% of prescribed drugs. For example, beta-blocker drugs prescribed for cardiac ailments target the β-adrenoreceptors − known GPCRs. The importance of GPCR biology was emphasised by the latest Nobel Prize in Chemistry (2012), awarded for studies of GPCRs.
Determining the structure of proteins and other biomolecules at the atomic level is central to understanding many aspects of biology. X-ray crystallography is the best known technique for structural biology but, as its name suggests, it only works with samples that can be crystallized. Electron cryo-microscopy (cryo-EM) can be used to determine atomic structures of biomolecules that cannot be crystallized, but until now achieving high-resolution cryo-EM structures has been difficult.
New research, from a team of scientists in the LMB’s Structural Studies Division and the EMBL-European Bioinformatics Institute, has uncovered how our genome keeps the effects of mutations in check. The discovery, published in the journal Cell, explains how new proteins are created, helping to deliver useful insights into the evolution of the human genome. The team’s findings may also help in improving our understanding of diseases such as cancer and neurodegeneration.