Protein clearance pathways and aggregate formation have recently been associated with dysfunctional biomolecular condensates. One protein commonly identified in aggregates in ALS is Sequestosome-1/p62. This study will combine proteomic, optogenetic and bioinformatic approaches to investigate how p62 biomolecular condensates are involved in ALS states. We aim to identify how p62 domains and ALS-linked proteins alter the interactome of p62 to disrupt its biomolecular properties, leading to protein aggregation. These studies will provide valuable insight into a newly described process in ALS and potentially identify a therapeutic target to be leveraged for ALS treatment.
|Effective start/end date
|14/03/23 → 14/03/24