The award is given to Dr. Varun Venkataramani (Heidelberg University Hospital, Germany). Varun grew up in Hannover, Germany, and studied medicine and bioscience at Heidelberg University. He obtained his medical degree (MD) in 2016 with highest distinction and completed his MD thesis in 2019 and his PhD thesis in 2020, both from Heidelberg University and both with summa cum laude honors, focusing on basic and cancer neuroscience.

After completing his postdoctoral research at the German Cancer Research Center in Heidelberg, he became a Junior Group Leader in the Department of Neurology at University Clinic Heidelberg in 2022, where he continues his pioneering work in neuroscience-instructed cancer therapy. His research has revealed groundbreaking insights into neuron-glioma synaptic contacts driving tumor growth, established neuronal mechanisms underpinning brain tumor invasion and pioneered technologies to investigate these multicellular cancer networks.

Dr. Venkataramani's work bridges neuroscience, oncology, and technology development. His research focuses on three fundamental objectives: methodological innovation in cancer neuroscience, mapping brain cancer connectomes, and establishing neuroscience-instructed cancer therapies as a cornerstone of oncological treatment.

He has received numerous awards for his work, including the Basic Science Award of the Society for Neuro-Oncology (2022), the Publication Prize of the Else-Kröner Fresenius Foundation (2023), and the BIAL Prize in Biomedicine (2024). As a neurologist and neuroscientist, Dr. Venkataramani continues to advance the field of cancer neuroscience, working towards improved treatments and outcomes for patients with brain tumors.

The brain's delicate network of neurons communicates through specialized junctions called synapses, enabling complex functions from memory formation to conscious thought. Our research has uncovered a startling phenomenon: brain cancer cells can integrate into this neural network by forming functional synapses with neurons. These neuron-to-cancer cell synapses represent a previously unknown mechanism by which brain tumors interact with their surrounding environment. We could demonstrate that glioblastoma, an aggressive brain cancer, receives direct synaptic input from neurons. These connections are not mere physical contacts but functional glutamatergic synapses that transmit electrical signals. Most surprisingly, this synaptic communication drives tumor growth and facilitates cancer cell invasion throughout the brain.

We pioneered methodologies to investigate neuron-tumor networks and multicellular cancer networks in general. By developing advanced imaging approaches we created new ways to visualize these interactions in living tissue with unprecedented resolution. Our lab has also established novel tracing methods to map the connectivity between neurons and cancer cells across the entire brain. By mapping the molecular architecture of these connections, we discovered that cancer cells express neurotransmitter receptors similar to those found in neurons and we identified cellular states within tumors that are particularly prone to connect with neurons. Our recent work further revealed that glioblastoma cells adopt neuron-like characteristics to navigate the brain, hijacking neuronal mechanisms to facilitate their spread. Looking forward, we remain committed to further developing technologies to visualize and map neuron-tumor connections across the entire brain, creating a comprehensive "cancer connectome." Understanding these networks may lead to novel therapeutic strategies that disrupt neuron-tumor communication, potentially overcoming the treatment resistance that characterizes brain tumors. .

Fena Ochs earned her Ph.D. in 2018 from the Novo Nordisk Foundation Centre for Protein Research at the University of Copenhagen. Under the mentorship of Professor Jiri Lukas, she identified a novel function for the tumor suppressor protein 53BP1 in DNA repair. Fena then joined the laboratory of Professor Kim Nasmyth at the University of Oxford as Postdoctoral Fellow. There, she deciphered the stoichiometry of the essential protein complex cohesin during cell division. Throughout her career, she has been developing cutting-edge super-resolution microscopy technology, instrumental in these discoveries. In 2023, Fena was appointed Principal Investigator and Associate Professor at the University of Copenhagen in Denmark. Her laboratory focuses on understanding the mechanisms that maintain genome integrity and how their dysregulation leads to diseases, particularly cancer and neurodevelopmental disorders.

Illuminating the cohesin complex during cell division

Cell division is the foundation of life, responsible for constructing our tissues, organs, and entire bodies. Each cell division is a delicate process, ensuring the accurate distribution of our genetic code from one mother cell to two daughter cells. This critical task is orchestrated by a group of proteins known as the cohesin complex. Cohesin holds together newly duplicated sister chromatids from their genesis during DNA replication until their segregation during mitosis, in a process called sister chromatid cohesion.

Despite its discovery nearly three decades ago, the molecular mechanism underlying sister chromatid cohesion remains incompletely understood. Utilizing single molecule super-resolution imaging in human cells, I have discovered the nature of cohesin mediating sister chromatid cohesion. Monomers of cohesin, in conjunction with an accessory factor called Sororin, entrap identical chromosomes and facilitate their symmetrical distribution to daughter cells. These mechanistic insights advance our understanding of how sister chromatid cohesion is established and have implications for conditions where this process is impaired, such as age-related infertility.

After studying at École Polytechnique, Juliette Fedry completed her PhD with Felix Rey at Institut Pasteur Paris. She identified the first known sperm-egg fusion protein, HAP2, and showed that it was homologous to viral fusion proteins. During her postdoc with Friedrich Förster at Utrecht University, she used cryo-electron tomography to visualize protein translocation into the endoplasmic reticulum. This work allowed the identification, quantification and spatial analysis of the different translocon variants on native membranes. Juliette next implemented Focused Ion Beam milling approaches to visualise translation in entire mammalian cells and its reorganization upon ribosome collision stress. These studies provided a framework for quantitative analysis of translation dynamics in situ.

My research combines functional and structural approaches across scales to address long standing questions in cell biology.

During my PhD, I identified HAP2 as the first eukaryotic gamete fusion protein and determined its crystal structure, revealing homology with viral fusion proteins.

As a postdoc, I developed my research towards larger length scales and native cellular contexts. I established a workflow for high-resolution subtomogram averaging in native human endoplasmic reticulum (ER) membranes. These results uncovered fundamental insights into how various types of nascent protein chains recruit different ER translocon complexes to enter the secretory pathway. I further developed FIB-milling approaches to visualize translation in intact mammalian cells, revealing that the elongation factor eEF1A remains bound to human ribosomes during proofreading after hydrolysis. This finding contributes to rationalise why the human ribosome operates slower than its bacterial counterpart.

I leveraged these methods to elucidate the effect of cellular stress on translation dynamics and on the remodelling of the nuclear membrane.

I recently started my group at the MRC LMB, where I develop an integrative approach to study the regulation of proteostasis networks in healthy and diseased mammalian cells.