Proteomics

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Profiling the Interactome of Folded-State Protein Filaments in Yeast


ABSTRACT: The formation of large polymeric structures without protein unfolding and aggregation, such as cytoskeletal and enzyme filaments, is crucial for normal cellular function. We term this type of assembly agglomerates. There are several agglomeration-associated diseases, such as sickle cell disease, caused by hemoglobin agglomeration. Nevertheless, it is still unknown whether there is a specific machinery to recognize protein agglomeration or whether it can be recognized by the general proteostasis machinery (e.g., by ubiquitin-dependent degradation). Here, we compared interactomes of wild-type proteins and their mutated counterparts prone to aggregation or agglomeration in yeasts. For this, we performed a pull-down followed by shotgun proteomics to identify proteins that interact with protein aggregates and/or agglomerates. We found that proteostasis machinery (chaperones mainly) actively interacts with protein aggregates, which is not the case for agglomerates. Despite their large size, they are not recognized by proteostasis machinery. Agglomerates remain mainly inert for other protein-protein interactions except for the interaction with several yeast proteins prone to agglomeration per se.

INSTRUMENT(S):

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Arseniy Lobov  

LAB HEAD: Emmanuel Doram Levy

PROVIDER: PXD052474 | Pride | 2025-08-21

REPOSITORIES: Pride

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