All articles tagged with #protein misfolding
Scientists from Ohio State University have discovered that T-cell exhaustion in cancer is caused by a stress response called TexPSR, driven by misfolded proteins. Blocking this pathway restores T-cell function and enhances immunotherapy effectiveness across various cancer types, offering a new approach to improve cancer treatments.
Protein misfolding and deposits in the brain are common factors in neurodegenerative diseases. Recent research explores the phenomenon of cross-seeding, where misfolded proteins from one disease can induce the aggregation of others. A study focused on the interaction between the prion protein and TDP-43 reveals how they collaborate to impact neurodegenerative diseases by triggering the clumping and inactivation of TDP-43. This new mechanism sheds light on how disease-associated prion proteins can affect physiological signaling pathways through cross-seeding.
Researchers at Goethe University Frankfurt have discovered how mitochondria communicate with the cell when under stress. Mitochondria release reactive oxygen compounds and block the import of protein precursors, causing them to accumulate in the cell. This triggers a chemical change in a protein called DNAJA1, which then interacts with the folding assistant HSP70. HSP70 takes care of the misfolded protein precursors, reducing its interaction with its regular partner HSF1. HSF1 is then released and can trigger the cell's anti-stress mechanism for the mitochondria. The study sheds light on the intricate signaling pathways between mitochondria and cells during times of stress.