S Proteasome:Structure and Function. F (o|¨ )rster F,E. Sakata. Encyclopedia of Biological Chemistry . 2013Forster, F., Sakata, E., 2013. 26S proteasome: structure and function. In: Lennarz, W.J., Lane, M.D. (
The 26S proteasome is the most complex ATP-dependent protease machinery, of ~2.5 MDa mass, ubiquitously found in all eukaryotes. It selectively degrades ubiquitin-conjugated proteins and plays fundamentally indispensable roles in regulating almost all major aspects of cellular activities. To serve as...
During the past two years, significant progress has been made in understanding the structure and function of the proteasome. Recent work has revealed the three-dimensional structure of the 700 kDa proteolytic complex at atomic resolution and elucidated its novel catalytic mechanism. Close relationships ...
and its corresponding phenotype can be investigated by means of two mass-spectrometry-based approaches that differ in principle. The first approach attempts to describe a phenotype mechanistically using the aggregated structure and function of the proteins or modules that constitute the underlying ...
We report the cryo-EM structure of the human 26S proteasome at an average resolution of 3.5 Å, allowing atomic modeling of 28 subunits in the core particle (CP) and 18 subunits in the regulatory particle (RP). The C-terminal residues of Rpt3 and Rpt5 subunits in the RP can be seen...
The 26S proteasome is formed by a regulatory particle (RP) that binds and processes ubiquitinated substrates and a core particle (CP) that hydrolyzes proteins into peptides1. CP inhibitors are used to treat hematological cancers but resistance mechanisms motivate new strategies for proteasome inhibitio...
26sproteasomeinwhichseveralregulatorysubunits associatewithit.The20scorecomolexismadeoffour seven-subunitringsstackedtog&&to formabarrel- shaoedcomolex.IntheoroteasomefromThermoalasnra ncidophilk, whichhas&enapivotalroleinelu&ating theproteasomestructureandcatalyticmechanism,thea- subunitsformthetwoouterandthe5...
26sproteasomeinwhichseveralregulatorysubunits associatewithit.The20scorecomolexismadeoffour seven-subunitringsstackedtog&&to formabarrel- shaoedcomolex.IntheoroteasomefromThermoalasnra ncidophilk, whichhas&enapivotalroleinelu&ating theproteasomestructureandcatalyticmechanism,thea- subunitsformthetwoouterandthe5...
physiology and leukemia. Moreover, WT-MLL1 has been found to be essential for MLL1-rearranged (MLL1-r) leukemia. Rigorous studies of such PPIs have been performed and much progress has been achieved in understanding their structures, structure–function relationships and the mechanisms for ...
Elec‑ tron microscopy revealed that these structures are abnormal, enlarged presynaptic swellings filled with mainly fibrous mate‑ rial with occasional peripheral, presynaptic active zones forming synapses. Immunofluorescence imaging then showed that a number of markers for aging and especially ...