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Such a modulation of proteasome activity is explained, at least in part, by the circadian expression of both Nuclear factor (erythroid-derived 2)-like 2 (Nrf2) and the proteasome activator PA28ab
The functional assays demonstrate that PA28beta inhibited cell growth, proliferation and malignancy of TE-1 cells. Among the differentially expressed proteins, PA28b is a potential tumor inhibitor
Naa10p suppresses 28S proteasome activity through interaction with PA28beta.
knockdown of PA28beta could enhance tumor invasion and metastasis, at least in part, through up-regulation of CLIC1 in gastric adenocarcinoma
PA28 selectively up-regulates the presentation of viral MHC class I epitopes and that down regulation PA28 in tumor cells results in impaired presentation of a human TRP2 tumor antigen.
Impaired expression of proteasome subunits is involved in the loss of HLA class I expression in human colon cancer cells.
Study clarifies the subunit composition and arrangement of PA28ab and provides key insights into the assembly of an asymmetric complex from two highly homologous subunits. Differential scanning fluorimetry experiments and activity assays classify PA28alpha4beta3 as most stable and most active, indicating that this assembly might represent the physiologically relevant species.
Increased PA28B expression is associated with viral myocarditis.
Nrf2-dependent induction of proteasome and Pa28alphabeta regulator are required for adaptation to oxidative stress.
demonstrate that PA28 and the proteasome immunosubunits use fundamentally different mechanisms to enhance the supply of MHC class I-binding peptides
the processing of antigens is regulated by two distinct pathways, one requiring PA28 and the other hsp90
PA28-associated proteasome preferentially digested within epitopic sequences of K(d), although correct C-terminal flankings were removed
An alternative splice pattern of the Psme2 (PA28b) gene, which encodes the beta subunit of the proteasome activator PA28, is characterized.
The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits\; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. This gene encodes the beta subunit of the 11S regulator, one of the two 11S subunits that is induced by gamma-interferon. Three beta and three alpha subunits combine to form a heterohexameric ring. Six pseudogenes have been identified on chromosomes 4, 5, 8, 10 and 13.
proteasome activator complex subunit 2
, proteasome activator subunit 2
, 11S regulator complex subunit beta
, activator of multicatalytic protease subunit 2
, protease (prosome, macropain) 28 subunit, beta
, proteasome (prosome, macropain) 28 subunit, beta
, proteasome activator 28 subunit beta
, 11S regulator complex beta subunit
, MCP activator, 31-kD subunit
, cell migration-inducing protein 22
, proteasome activator 28-beta
, proteasome activator hPA28 subunit beta
, PA28 beta subunit
, proteasome activator 28 beta subunit