Proteasomes are protected from autophagic elimination upon carbon starvation by sequestration into cytoplasmic storage granules, which aid cell fitness by providing a cache of proteasomes that can be rapidly remobilized when carbon availability improves.
One α-synuclein strain inhibited proteasome activity and induced apparent pathologies, while the other did not, indicating a strain-dependent toxicity of α-synuclein aggregates, which support a prion-like behavior of α-synuclein.
The 26S proteasome lid subcomplex acts as an external scaffold whose interactions with the ATPase motor stabilize the substrate-engagement-competent state, and control conformational changes upon engagement for subsequent degradation steps.
Phototrophic growth laws are elucidated by combining computational modeling and experiments for quantitative evaluation of cellular physiology, morphology and proteome allocation across a wide range of light conditions.
An aspartyl protease is essential for the lytic cycle of Toxoplasma gondii and is involved in the maturation of proteins critical for invasion and egress, and it can be targeted selectively with an ethylamine scaffold based peptidomimetic inhibitor.