🔧 Flexibly assembled: Proteasomes, the cells’ garbage cans, are assembled in different ways
A new study by University Potsdam and the #UniCologne shows that the assembly of the proteasome, a central component of cellular protein quality control, does not follow a rigid program but uses flexible pathways. This discovery challenges established views in research.
📰 https://www.nature.com/articles/s41467-026-70525-w
#uniköln #unicologne #Proteasome #ProteinResearch #CellBiology
Derailed Protein Turnover in the Aging Mammalian Brain | presented by Jeffrey Savas, PhD
pulse-chase studies of long-lived proteins in mice
11:34 - distribution of extremely long lived proteins in tissues & organelles
27:44 - protein turnover is reduced in male aged brains, but elevated in female aged brains
30:43 - sex specific distinct cellular components have hampered protein turnover during aging (synapse, mitochondria, myelin sheath)
33:56 - proteasome activity during aging correlates with catalytic subunit turnover
36:00 - proteasome activity highest at 18 months (mice), correlates with turnover of catalytic subunits
https://youtu.be/-K0HjCJXQlg?si=XFakvMV5dv9qgMSU
#aging #brain #proteasome #proteomics #neuroscience #SexDifferences
Regulation of the proteasome is disrupted in the rare genetic disease known as NGLY1 deficiency. This manuscript finds that proteasome dysfunction in NGLY1-deficient C. elegans depends on nucleotide availability, indicating an unexpected regulatory crosstalk between nucleotide metabolism and protein turnover, and suggesting that interventions to alter nucleotide availability might mitigate proteasome insufficiency in diseases associated with proteasome dysfunction.
Protein quality control pathways play important roles in resistance against pathogen infection. This study shows that proteasome regulation keeps innate immune responses in check in a tissue-specific manner, against natural eukaryotic pathogens of the C. elegans epidermis and intestine.
Proteasomes and autophagy constitute the two main proteolytic machineries for cytoplasmic content. This Primer explores a new study in PLOS Biology which demonstrates that autophagy stimulation alters proteasome composition, degrading hyperactive immunoproteasomes and thereby limiting inflammation.
This #review summarises how pathogenic #effectors can mimic or target the highly conserved #ubiquitin–#proteasome system to disrupt cellular processes in their #plant hosts.
Presenting a model for proteasome condensate formation in which shuttle factors play a critical role. ↔ 💧
Kenrick Waite and team #KUMedCenter show that shuttling factors Rad23 and Dsk2 contribute to the localization of proteasomes in condensates - a process that Ddi1 counteracts. #preprint
#preLight by Aniruddha Das 👉 https://prelights.biologists.com/highlights/proteasome-condensate-formation-is-driven-by-multivalent-interactions-with-shuttle-factors-and-k48-linked-ubiquitin-chains/
Global histone H2B degradation regulates #insulin/#IGF signaling-mediated nutrient stress
The #ubiquitin-#proteasome system regulates #histone #H2B exchange in mammalian cells and in C. elegans during development and starvation.
24-AUG-2023
Scientists discover a previously unknown way cells break down proteins
The mechanism degrades short-lived proteins that support brain and immune functions
https://www.eurekalert.org/news-releases/998812
a new way of dragging them into the proteasome, to be precise. I assume the proteasome will still digest them the good old way.
Universität zu Köln
Rhyothemis
PLOS Biology
Journal of Experimental Botany
preLights
The EMBO Journal
michael