EXTRAORDINARY IBMB SEMINAR, Friday, April 19th 10:00 AM | Dr. Rubén Fernández-Busnadiego

Recent technological developments, such as direct electron detectors and cryo-focused ion beam milling, allow cryo-electron tomography (cryo-ET) to image cells with unprecedented resolution. My group capitalizes on these advances to investigate the structural basis of cell function and pathological dysfunction in situ. In this talk, I will discuss (i) the basics of cryo-ET technology, (ii) our recent data shedding light into the toxic roles of protein aggregation in neurodegenerative diseases [see e.g. 1, 2, 3], and (iii) the perspectives of our future work.

Ruben studied Physics at the Complutense University of Madrid (Spain). Afterwards, he carried out a research fellowship in the lab of Marcellus Ubbink at Leiden University (The Netherlands), which sparked his curiosity for structural biology. For his PhD, he joined the department of Wolfgang Baumeister at the Max Planck Institute of Biochemistry (Germany), where he investigated the structure of the presynaptic terminal by cryo-electron tomography (cryo-ET) [see e.g. Fernandez-Busnadiego et al., J Cell Biol 2010, 2013]. To dive deeper into the molecular mechanisms of neuronal function, he worked with Pietro De Camilli (Yale University, USA) as a postdoctoral fellow [see e.g. Fernandez-Busnadiego et al., PNAS 2015]. Later, he returned to the Max Planck Institute of Biochemistry to start a group using cryo-ET to investigate in situ the structure of toxic protein aggregates within cells. This work provided important insights into the structural mechanisms underlying neuronal death in neurodegenerative diseases [see e.g. Bäuerlein et al., Cell 2017; Guo et al., Cell 2018; Guo et al., Nature 2018; Trinkaus et al., Nat Comm 2021; Riemenschneider et al., EMBO Rep 2022]. In 2019, he joined the faculty of the University Medical Center Göttingen (Germany), where he continues to harness the latest electron microscopy technology to unravel the structural basis of cell function and pathological dysfunction.