Protein aggregates, and in particular amyloids, are generally considered to be inherently irreversible aberrant clumps, and are often associated with pathologies, such as Alzheimer's disease, Parkinson's disease, or systemic amyloidosis. However, recent evidence demonstrates that some aggregates are not only fully reversible, but also perform essential physiological functions. Despite these new findings, very little is known about how these functional protein aggregates are regulated in a physiological context. Here, we take the yeast pyruvate kinase Cdc19 as an example of a protein forming functional, reversible, solid, amyloid-like aggregates in response to stress conditions. Cdc19 aggregation is regulated via an aggregation-prone low complexity region (LCR). In favorable growth conditions, this LCR is prevented from aggregating by phosphorylation or oligomerization, while upon glucose starvation it becomes exposed and allows aggregation. We suggest that LCR phosphorylation, oligomerization or partner-binding may be general and widespread mechanisms regulating LCR-mediated reversible protein aggregation. Moreover, we show that, as predicted by computational tools, Cdc19 forms amyloid-like aggregates in vitro. Interestingly, w...Continue Reading
The HET-s prion protein of the filamentous fungus Podospora anserina aggregates in vitro into amyloid-like fibrils
Kinetics of the thermal inactivation and aggregate formation of rabbit muscle pyruvate kinase in the presence of trehalose
Antimicrobial protegrin-1 forms amyloid-like fibrils with rapid kinetics suggesting a functional link
Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels
Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies
The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis
Thioflavin-S staining coupled to flow cytometry. A screening tool to detect in vivo protein aggregation
Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation
Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains
PKM2 isoform-specific deletion reveals a differential requirement for pyruvate kinase in tumor cells
Phosphorylation-regulated binding of RNA polymerase II to fibrous polymers of low-complexity domains
A super-assembly of Whi3 encodes memory of deceptive encounters by single cells during yeast courtship
Filament formation by metabolic enzymes is a specific adaptation to an advanced state of cellular starvation
Regulation of Functional Protein Aggregation by Multiple Factors: Implications for the Amyloidogenic Behavior of the CAP Superfamily Proteins.
High-throughput multiparametric imaging flow cytometry: toward diffraction-limited sub-cellular detection and monitoring of sub-cellular processes.
Amyloid-like Prep1 peptides exhibit reversible blue-green-red fluorescence in vitro and in living cells.
The less conserved metal-binding site in human CRISP1 remains sensitive to zinc ions to permit protein oligomerization.
Alzheimer's Disease: Amyloid Beta
Alzheimer's disease is a neurodegenerative disease associated with the accumulation of amyloid plaques in the brain; these plaques are comprised of amyloid beta deposits. Here is the latest research in this field.
Alzheimer's Disease: APP
Amyloid precursor protein (APP) proteolysis is critical for the development of Alzheimer's disease, a neurodegenerative disease associated with accumulation of amyloid plaques in the brain. Here is the latest research on APP and Alzheimer's disease.