, 14 June 2016 How cells bag their rubbish The buildup of protein deposits in cells is a hallmark of neurodegenerative diseases such as Alzheimer’s and Parkinson’s. “A protein accumulates in neurons, neurons die, and patients gradually lose brain functions,” says Carsten Sachse from EMBL. “If the process by which the cell removes those proteins can be enhanced, then you might be able to prevent that disease progression.” Before scientists can give the cell’s rubbish collectors a boost, they have to understand how the system works. In a paper recently published in EMBO Reports, Sachse and his lab drew on expertise from colleagues throughout EMBL to do just that.
Heidelberg, 20 May 2016 Making cells move towards the light An airplane leaving a lit-up runway is not the image you’d expect to see on the cover of a scientific journal, but there it is on this month’s issue of Cell Chemical Biology. Inspired by a study from Carsten Schultz’s lab, the image draws on the idea of using light to direct movement. The scientists developed a new way to switch on a lipid called LPA, which many cells – including cancer cells – are known to move towards. They manipulated this molecule so that it only becomes active when they shine a light on it. With this new method, researchers can make cells move towards a particular place, by flipping a switch.
Heidelberg, 17 May 2016 Unexpected link in protein production I shared a room at a conference in Baeza, Spain, in November 2013 with Zoltan Villanyi from the University of Geneva. As we sat in the same talks, we quickly found that we had the same questions for speakers, and discovered that we’d been given spots next to each other during the poster presentation – that’s where we got really interested in each other’s work. We stayed in touch, and began to work together the following month, exchanging a few RNA samples for sequencing. From there, the collaboration bloomed. In the end, what we found – and recently published in Cell Reports – was quite surprising.
Hamburg, 10 May 2016 Enzyme with a dual-purpose loop A closer look at the 3D molecular structure of Death Associated Protein Kinases (DAPK) reveals an unexpected dual-purpose loop in the folded string of amino acids. Work by researchers in the Wilmann’s group at EMBL Hamburg, published in Structure, suggests that the small loop is crucial for dimer formation and calmodulin binding. “What started as a small side project, unearthed a complex and important signaling pathway within this group of kinases,” says Matthias Wilmanns, “It goes to show, you can’t always plan science!”
Hinxton, 2 May 2016 Breast cancer study: towards personalised treatment The largest-ever study to sequence the whole genomes of breast cancers has uncovered five new genes associated with the disease and 13 new mutational signatures that influence tumour development. Published in Nature and Nature Communications, two studies from the Wellcome Genome Campus pinpoint where genetic variations in breast cancers occur. The findings provide insights into the causes of breast tumours and demonstrate that breast-cancer genomes are highly individual.
Heidelberg, 28 April 2016 Poo transplants better understood For the first time, scientists studying stool transplants have been able to track which strains of bacteria from a donor take hold in a patient’s gut after a transplant. The team led by the Bork group found that compatibility between donor and patient likely plays a bigger role in these transplants than previously thought. The study, published in Science, could help make stool transplants a valid treatment option for more conditions than they are currently applied to.
Heidelberg, 14 April 2016 EMBL scientists reveal structure of nuclear pore’s inner ring It was a 3D puzzle with over 1000 pieces, with only a rather fuzzy outline as a guide. But scientists in the Beck group at EMBL have now put enough pieces in place to see the big picture. In a study published today in Science, they present their latest findings, bringing the nuclear pore complex into focus.
Monterotondo, 7 April 2016 Welcome: Hiroki Asari New group leader Hiroki Asari seeks to unpick connections between sight and mind, answering questions such as why a cookie looks different depending on how hungry you are. The Asari group will be studying how the visual system is influenced by state of body and mind. They will present the same set of visual stimuli to mice in different situations. By combining such experiments with computer modelling, they aim to reconstruct the circuitry of neurons in the eye and the brain, and the connections between them. “Our visual system works way better than the state-of-the-art computer systems – it’s just amazing!” he says.
Heidelberg, 31 March 2016 Designing gene therapy Scientists in the Barabas group at EMBL have increased the efficiency of a genome-engineering tool called Sleeping Beauty, which is showing promise in clinical trials for leukaemia and lymphoma immunotherapies. They made the improvement by determining the 3-dimensional structure of the molecule’s active domain, and using that information to design better versions of this tool. In a study published in Nature Communications, they reveal structural information that they hope will ultimately result in better patient outcomes.
Hinxton, 24 March 2016 Foetus, or placenta? When exactly does an embryonic cell decide whether it will become part of the foetus, or part of the placenta? Scientists at the University of Cambridge and in the Marioni group at EMBL-EBI shed light on this important question by studying the development of mice embryos only four cells in size. The findings, published in Cell, show subtle differences between seemingly identical cells at a very early stage of development, and have implications for the understanding of mammalian development.