MRC Laboratory of Molecular Biology
One of the world's leading research institutes, our scientists are working to advance understanding of biological processes at the molecular level - providing the knowledge needed to solve key problems in human health.
Recent work carried out by David Komander’s group in the LMB’s Protein and Nucleic Acid Chemistry Division, and published in two separate papers, has provided insight into human disease and the role played by ubiquitination, a process that affects many fundamental cellular processes.
Work in David’s group aims to understand the cellular machinery for specific ubiquitin (Ub) assembly, disassembly, and binding on a structural and biochemical level.
Work published in the journal Structure by Kiyoshi Nagai’s group in the LMB’s Structural Studies Division, has provided further detailed information on the structure and role of proteins at the active site of the spliceosome, and may also help to explain the molecular pathology of the eye disease, retinitis pigmentosa type 13 (RP13).
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.
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 [1].