GRASPing the unconventional secretory machinery to bridge cellular stress signaling to the extracellular proteome
Authors:Constantinos Demetriades1,2, Julian Nüchel1 and Markus Plomann3
1 Max Planck Institute for Biology of Ageing (MPI-AGE), 50931 Cologne, Germany.
2 University of Cologne, Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), 50931 Cologne, Germany.
3 University of Cologne, Faculty of Medicine and University Hospital Cologne, Center for Biochemistry, 50931 Cologne, Germany.
Keywords:
mTORC1, unconventional protein secretion (UPS), GRASP55, Tuberous Sclerosis Complex (TSC), cellular stress response, Golgi, rapamycin.
Corresponding Author(s):
Conflict of interest statement:
The authors declare no competing interests.
Please cite this article as:
Constantinos Demetriades, Julian Nüchel and Markus Plomann (2021). GRASPing the unconventional secretory machinery to bridge cellular stress signaling to the extracellular proteome. Cell Stress 5(11): 173-175. doi: 10.15698/cst2021.11.259
© 2021 Demetriades et al. This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduc-tion in any medium, provided the original author and source are acknowledged.
Abstract:
Cellular adaptation to stress is a crucial homeostatic process for survival, metabolism, physiology, and disease. Cells respond to stress stimuli (e.g., nutrient starvation, growth factor deprivation, hypoxia, low energy, etc.) by changing the activity of signaling pathways, and interact with their environment by qualitatively and quantitatively modifying their intracellular, surface, and extracellular proteomes. How this delicate communication takes place is a hot topic in cell biological research, and has important implications for human disease.