DescriptionThe proteasome degrades most cellular proteins in a tightly regulated manner and thereby controls virtually all cellular processes. Proteasome is hence vital in all organisms and cells having dysfunction in proteasomal degradation are known to accumulate misfolded, mutated, and damaged proteins in the form of insoluble aggregates. This failure of maintaining a functional proteome is associated with a broad range of humans diseases, including neurodegeneration and cancer. While the contribution of the dysfunction of the proteasome in disease is well-appreciated, the underlying mechanisms are often unknown. Thus, understanding how cells adapt protein degradation to meet their requirements and how it is affected under challenging conditions is of great importance. We recently discovered that under nutrient deprivation, the translation of proteasome assembly chaperones (PACs) is induced, therefore increasing the assembly of functional proteasomes. Mechanistically, we found that PAC mRNAs travels along actin cables but upon different stresses, actin cables are disrupted and the mRNA relocalises to cortical actin patches (dense networks of branched actin filaments localised at the plasma membrane). This dynamic mRNA relocalisation process is important for PAC mRNAs translation (Williams et al., Nat. Cell Biol., 2022). Together these findings illustrate that actin remodelling is important for regulating the localisation and translation of stress-induced proteins such as PACs to maintain proper proteasome homeostasis.
|Period||7 Nov 2022|
|Event title||Applied Microbiology 2022|
|Location||Paris, FranceShow on map|