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In an international research collaboration involving the University Medical Center Göttingen (UMG), researchers have produced the most complete map to date of how long different proteins persist in many tissues of the body. They were able to identify a mechanism that increases the stability of proteins and thus favors neurodegenerative diseases such as Alzheimer's and Parkinson's disease. The results have been published in the renowned scientific journal Cell.
Proteins ensure that human cells function and are viable. Proteins are formed to perform a specific task in the cell and once this task has been completed, they are broken down again. If this process is disrupted, diseases such as Parkinson's or Alzheimer's can develop. Both diseases are characterized by the destruction of nerve cells in the brain and are therefore referred to as neurodegenerative diseases. While Parkinson's disease leads to movement disorders such as trembling, slowed movements, balance problems and stiffened muscles, Alzheimer's disease manifests itself in increasing memory problems and perceptual disorders, among other things. In both cases, the cause is that old and damaged proteins are not broken down properly, accumulate in the cells and clump together. These protein clumps, also known as aggregates, can no longer be broken down by the body and ensure that the nerve cells are gradually destroyed.
In an international collaboration involving the University Medical Center Göttingen (UMG), Dr. Eugenio F. Fornasiero, group leader at the UMG's Department of Neuro- and Sensory Physiology, and his US colleagues from Yale University in New Haven, Connecticut, and St. Jude Children's Research Hospital in Memphis, Tennessee, have produced the most complete map to date of how long different proteins persist in many tissues of the body. “This extensive data set is like a blueprint for understanding how different organs manage their proteins,” says Dr. Fornasiero, one of the study's last authors. “We can see which proteins are turned over quickly in the brain, for example, and which ones persist longer - this gives us clues about their stability and their role in neurodegenerative diseases.”
The researchers discovered that a mechanism that switches proteins 'on' and 'off' also plays a role in the stabilization of proteins: protein phosphorylation. In this process, phosphate groups are transferred to proteins, which leads to the corresponding protein being switched on, i.e. activated. Removing the phosphate groups switches the protein off. In the brain tissue of mice suffering from Alzheimer's disease, for example, the scientists were able to show that the protein “Tau”, which is involved in the development of the disease, is increasingly phosphorylated in certain sections. This increases the stability of the Tau protein and prolongs its lifespan. This in turn promotes the formation of protein aggregates and the death of nerve cells.
“Understanding how phosphorylation influences the stability and turnover of proteins could help to develop new therapeutic strategies for the treatment of Parkinson's and Alzheimer's disease. For example, by preventing or reversing such pathological changes,” says Fornasiero. In addition to identifying disease-relevant proteins, understanding protein turnover and its regulation also helps to identify those proteins that are particularly susceptible to ageing processes. This also opens up new avenues for future anti-ageing therapies.
The results have been published in the renowned scientific journal Cell.
Original publication:
Wenxue Li, Abhijit Dasgupta, Ka Yang, Shisheng Wang, Nisha Hemandhar-Kumar, Surendhar R. Chepyala, Jay M. Yarbro, Zhenyi Hu, Barbora Salovska, Eugenio F. Fornasiero, Junmin Peng and Yansheng Liu. An Extensive Atlas of Proteome and Phosphoproteome Turnover Across 2 Mouse Tissues and Brain Regions. Cell (2025). DOI: https://doi.org/10.1016/j.cell.2025.02.021
More than 256,000 phosphorylation sites of various proteins were analyzed in this study, providing an unprecedented view of how proteins are maintained and replaced throughout the body, even across different activity states. “This is important not only because it allows us to understand how activity can affect protein stability, but also because it reveals the intricate balance of molecular renewal. Similar to how a city's infrastructure is constantly repaired and upgraded to keep everything running smoothly, this dataset shows in detail where and when molecular 'renovations' take place and how they ultimately shape the landscape of cells,” says Fornasiero.
University Medical Center Göttingen, University of Göttingen
Department of Neuro- und Sensory Physiology
Dr. Eugenio F. Fornasiero
Humboldtallee 23, 37073 Göttingen
Phone +49 551 / 39-67930
eugenio.fornasiero@med.uni-goettingen.de
fornasierolab.uni-goettingen.de
Wenxue Li, Abhijit Dasgupta, Ka Yang, Shisheng Wang, Nisha Hemandhar-Kumar, Surendhar R. Chepyala, Jay M. Yarbro, Zhenyi Hu, Barbora Salovska, Eugenio F. Fornasiero, Junmin Peng and Yansheng Liu. An Extensive Atlas of Proteome and Phosphoproteome Turnover Across 2 Mouse Tissues and Brain Regions. Cell (2025). DOI: https://doi.org/10.1016/j.cell.2025.02.021
Artistic representation of proteins (blue), whose formation and degradation is symbolized by the clo ...
hassan tahini
Dr. Eugenio F. Fornasiero, research group leader at the Department of Neuro- and Sensory Physiology ...
dennis reichert, www.kanalvier.de
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