Deubiquitination Reactions on the Proteasome for Proteasome Versatility

The proteasome

How does it work? The proteasome consists of a cylindrical 20 S catalytic chamber (see Figure), capped on one or both ends by a 19 S regulatory complex. The regulatory complex (which is made of at least 18 different subunits, six of which are ATPases; not shown in the Figure) recognizes ubiquitinated proteins and is thought to drive their unfolding, although the mechanism is not understood. The...

Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome.

The 26S proteasome mediates degradation of ubiquitin-conjugated proteins. Although ubiquitin is recycled from proteasome substrates, the molecular basis of deubiquitination at the proteasome and its relation to substrate degradation remain unknown. The Rpn11 subunit of the proteasome lid subcomplex contains a highly conserved Jab1/MPN domain-associated metalloisopeptidase (JAMM) motif-EX(n)HXHX...

Modelling Proteasome and Proteasome Regulator Activities

Proteasomes are key proteases involved in a variety of processes ranging from the clearance of damaged proteins to the presentation of antigens to CD8+ T-lymphocytes. Which cleavage sites are used within the target proteins and how fast these proteins are degraded have a profound impact on immune system function and many cellular metabolic processes. The regulation of proteasome activity involv...

PKG primes the proteasome.

The Proteasome Pathway Destabilizes