Insight on Research


Watching neurons transmit visual information

Work in Leon Lagnado’s group in the LMB’s Neurobiology Division is showing how synapses transmit visual signals in the retina of zebrafish. The group designed fluorescent proteins that light up when synapses are active and made transgenic zebrafish expressing these proteins in retinal neurons. They then used a multiphoton microscope to directly observe the activity of synapses in the retina of live fish as they responded to different visual stimuli.

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New mechanism in the body’s timekeeping revealed

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.

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Understanding the mechanism of the nucleocytoplasmic transport cycle

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.

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TRIM21 senses infection and triggers immune response inside cells

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 [1].

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Uncovering molecular signatures of G-protein-coupled receptors

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.

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Ribosome structure determined to near-atomic resolution by cryo-EM

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.

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The guardian of the transcriptome

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.

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Salt chemosensation in worms linked to human deafness

Transmembrane channel-like (TMC) genes encode a conserved family of predicted membrane proteins in animals. The founding member, human Tmc1, is strongly linked to deafness, being expressed in cochlear hair cells and known to be required for their function. However, the precise molecular function of these proteins has until now been unknown.

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Architecture of the spliceosome active site

Research in the group of Kiyoshi Nagai in the LMB’s Structural Studies Division has for the first time provided detailed information on the structure and role of proteins at the active site of the spliceosome, which is responsible for the excision of introns from messenger-RNA (mRNA) precursors in the nucleus.
The spliceosome is a large and dynamic RNA-protein assembly.

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