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MRC Laboratory of Molecular Biology

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.

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TMEM106B filaments form in an age-dependent manner in human brains

Inter-divisional collaboration between the groups of Sjors Scheres, Michel Goedert and others identified TMEM106B as a new protein responsible for amyloid filament formation, and showed that these filaments develop in an age-dependent manner in human brains.

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Published on 28th March, 2022

Structural study reveals a novel activation mechanism for the fungal GPCR, Ste2

Structural snapshots of the Class D GPCR dimer, Ste2 (blue, green), along its activation pathway using cryo-EM. This provides a detailed picture, revealing a fundamentally different activation mechanism to previously-known GPCRs.

Chris Tate’s group, in the LMB’s Structural Studies Division, have used cryo-EM analysis to show that Ste2, a fungal Class D GPCR, has a fundamentally distinct activation mechanism in comparison to other types of GPCRs.

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Published on 16th March, 2022

Cryo-EM structures reveal molecular basis of human telomerase recruitment

Cartoon-like image of two hands (representing TPP1 and POT1) pulling on a rope (representing DNA) to illustrate how these proteins assist telomeric DNA binding to telomerase (represented as a newly discovered cryo-EM structure).

Kelly Nguyen’s group in the LMB’s Structural Studies Division has determined the molecular basis of how the TPP1 and POT1 components of shelterin recruit human telomerase to telomeres and regulate the enzyme’s activity during genomic replication.

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Published on 25th February, 2022

New method to discover protease and other hydrolase substrates in live mammalian cells

Using genetic code expansion techniques, Jason Chin’s group in the LMB’s PNAC Division have designed a new mechanism-based, light-activated technique to trap and identify new protease and other hydrolase substrates.

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Published on 17th February, 2022

Cryptochrome proteins are integral to maintain time within the brain’s master clock

Schematic using confocal microscopy (upper images) shows the localisation of fluorescently-tagged, endogenous PER2 (green), present in the nuclei of SCN neurons (blue). In the absence of CRY proteins, PER2 was instead localised predominantly within the cytoplasm and exhibited greater overall intracellular mobility (middle schematic), with absence of rhythmicity in SCN brain slices (lower schematic). Resuming CRY expression to a critical threshold only partially relocalised PER2 protein to the nucleus, yet was sufficient to fully restore rhythmicity to SCN brain slices (right most panels).

Using synthetic biological techniques, Michael Hastings’ group have collaborated with Jason Chin to gain novel insights into the molecular and cellular processes which govern the suprachiasmatic nucleus, and identified a key regulatory role of cryptochrome clock proteins.

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Published on 20th January, 2022

Atomic structures of Aβ42 filaments from the brains of individuals with Alzheimer’s disease and other neurodegenerative conditions

Atomic structure for Type I (Left) and Type II (Right) of amyloid-β 42 filaments

Collaboration between Sjors Scheres’ (Structural Studies), Benjamin Ryskeldi-Falcon’s and Michel Goedert’s (both Neurobiology) groups have used cryo-EM to reveal structures of Aβ42 filaments, the key factor behind the pathogenesis of Alzheimer’s disease.

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Published on 14th January, 2022
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