Sascha Martens elected EMBO member: “I’m looking forward to helping support young scientists”
The EMBO (European Molecular Biology Organization) membership honours distinguished scientists who have made outstanding contributions in the field of the life sciences. Members can actively participate in EMBO’s initiatives by serving on the organisation's Council, committees and editorial boards, participating in the evaluation of applications for funding, and by acting as mentors for young scientists.
Three DOC fellowships for Max Perutz Labs students
Konstantina Georgiou, Sara Scinicariello, and Ameya Rakesh Khandekar have been awarded DOC fellowships by the Austrian Academy of Sciences (ÖAW) that will support their PhD projects, which focus on genome organization, protein degradation, and RNA biology respectively.
Cep97: a stabilizing protein roof for centrioles
The proposed function of the centriolar protein Cep97 has to be revised, a new study from the Dammerman lab shows. Rather than just limiting centriole elongation, Cep97 forms a protective roof that ensures that centrioles maintain their correct size once the proper length is reached. The findings are published in “Current Biology” and could help explain how centrioles maintain their size and stability through multiple cell divisions, often throughout the entire lifetime of an organism.
A “DEEP-Clear” view of nervous system diversity
Researchers from the lab of Florian Raible at the Max Perutz Labs and their collaborators have developed an improved tissue clearing and depigmentation method that will help scientists to apply advanced microscopy methods to larger model organisms. The approach, termed “DEEP-Clear” and published in the journal Science Advances, is expected to improve scientists’ ability to study and visualize the whole nervous systems of many different species.
Happy - virtual - birthday, Max Perutz!
Birthdays should be celebrated, even in challenging times. Last year marked the inaugural celebration of the birthday of Max Perutz, the man who gave the Perutz Labs its name. Unfortunately, preparations for this year´s Max Perutz Day on May 19th were put on ice due to COVID-19. Nevertheless, we did not want this day to pass without celebrating a “virtual Max Perutz Day 2020” online with an outstanding keynote speaker: Jan Löwe, director of the MRC Laboratory of Molecular Biology (LMB) in Cambridge. Jan shared his personal memories of Max Perutz and talked about his own research in the field of structural biology.
“Reverse engineering” autophagosome biogenesis reveals new protein interactions
Scientists from Sascha Martens Lab at the Max Perutz Labs and their colleagues from the University of Berkeley (USA) have reconstituted the activity of key proteins involved in the growth of autophagosome precursors, a process essential for encapsulating cellular components targeted for degradation and recycling. Their results reveal a previously unknown positive feedback loop and activation mechanism that help explain how the autophagy machinery rapidly generates the autophagosomal membrane. The study is published in the Journal of Cell Biology.
Alwin Köhler appointed as Scientific Director
On March, 21st, 2020, Alwin Köhler was announced as the new Director of the Max Perutz Labs Vienna. He holds a joint Professorship for Molecular Biology at the University of Vienna and the Medical University of Vienna.
A Broad Alliance of Viennese Scientists builds COVID-19 Testing Infrastructure
The COVID-19 pandemic poses an enormous threat for healthcare systems and economies in Austria, Europe and the world. In this time of crisis, scientists in Vienna are responding to the threat. 20 research institutions have joined forces to form the Vienna COVID-19 Detection Initiative (VCDI). This initiative is now putting a new diagnostics pipeline into operation. The VCDI is also developing a range of high-throughput tests to better understand and combat the virus.
Layered Liquids – reaction chambers for gene regulation
A marvel of complexity, the nucleus is the command center of the cell – harboring information, codes and controlled access. But different from man-made command centers, the nuclear interior looks chaotic to the eye of a scientist. Chromosomes, the carriers of genetic information, float amidst a sea of water, proteins, nucleic acids and other molecules, all engaged in a myriad of simultaneous reactions. These reactions have one major goal: to turn genes on and off at the right time and place. This process is called gene regulation and makes a brain cell look and act different from a muscle cell or a liver cell.
Frameshifts could be evolutionary shortcuts to create novel proteins
Frameshifts occur when the reading frame in which genetic information is translated is perturbed. Textbook knowledge considers frameshifts to be dangerous as they typically result in altered protein sequences, which are frequently also truncated. Recent research from the lab of Bojan Zagrovic shows that even though frameshifts change the protein sequence, several of its important physicochemical properties stay the same. The results point to a possible new role for frameshifts: They may be a conserved strategy for evolution to create novel protein sequences with already optimized physicochemical properties.
Selma Osmanagic-Myers is Researcher of the Month at the Medical University of Vienna
The Medical University of Vienna has nominated Selma Osmanagic-Myers as Researcher of the Month March 2020 for her paper „Endothelial progerin expression causes cardiovascular pathology through an impaired mechanoresponse”. In this work, published in 2018 in the renowned journal “JCI”, she showed that endothelial cells of progeria patients fail to cope with the mechanic stress caused by bloodflow. This activates signaling mechanisms that lead to cardiovascular diseases. Selma studied biochemistry in Vienna and later joined the lab of Roland Foisner at the Max Perutz Labs as a Postdoc. She just recently moved to the Center of Pathobiochemistry and Genetics at the Medical University where she will continue her work on the impact of aging on endothelial cells, especially in the premature aging disease Hutchison Gilford Progeria.
Mechanism of inactivation of the tumor suppressor PP2A: an illusion shattered by reality
Protein Phosphatase 2 (PP2A) is an enzyme that plays important roles in regulating cell proliferation and by that has been shown to be a tumor suppressor. Inactivation of PP2A has been observed in many diseases including cancer. Egon Ogris and his team have now found out that the prevailing model of PP2A inactivation by phosphorylation needs to be revised. Notably, decades of research on the tumor suppressive function of PP2A were based on antibodies that - as it turns out now - do not recognize phosphorylation but are rather blocked by a completely different post-translational modification.
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