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Study shows that chronic exposure to cocaine alters the nuclear levels of PSMC5, an ATPase-containing subunit of the 19S proteasomal complex, in the nucleus accumbens and that PSMC5 in turn controls behavioral responses to cocaine.
These results imply that a deficiency in 19S Rpt6 may be partially related to the MPTP-induced increase in alpha-synuclein in the striatum. (19S Rpt6)
Caspase-3 (show CASP3 Proteins) cleaves specific 19 S proteasome subunits in skeletal muscle stimulating proteasome activity
autoinflammation-associated H443P nlrc4 (show NLRC4 Proteins) mutant is altered in interaction with SUG1 and ubiquitinated proteins, triggering constitutive caspase-8 (show CASP8 Proteins)-mediated cell death dependent on FADD (show FADD Proteins) but independent of Ser (show SIGLEC1 Proteins)(533) phosphorylation.
results demonstrate that PSMC5 is a new and important player involved in regulating ERK1/2 signal transmission through the remodeling of Shoc2 (show SHOC2 Proteins) scaffold complex in a spatially-defined manner.
Our data suggest that PSMC5 facilitates the damaging effects of radiation in radiation-responsive H460 cancer cells and therefore may serve as a prognostic indicator for radiotherapy and molecular targeted therapy in lung cancer patients.
TRIP-1 regulates fibroblast acquisition of phenotype and function associated with myofibroblasts.
gamma-aminobutyric acidB receptor proteasomal degradation is mediated by the interaction of the GABAB2 C terminus with the proteasomal ATPase Rtp6 and regulated by neuronal activity
Rpt6 interacts directly with CKIP-1 (show PLEKHO1 Proteins) and promotes the turnover of Smurf1 (show SMURF1 Proteins).
Sug1 plays a critical role in transcription of MHC class I, and the MHC class II-like molecules, HLA-DM and HLA-DO.
Findings show that Sug1 is crucial for regulating histone H3K4me3 and H3R17me2 at the cytokine inducible MHC-II and CIITA (show CIITA Proteins) promoters.
SUG1 has a role in ubiquitin/proteasome-mediated degradation of estrogen receptors
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. This gene encodes one of the ATPase subunits, a member of the triple-A family of ATPases which have a chaperone-like activity. In addition to participation in proteasome functions, this subunit may participate in transcriptional regulation since it has been shown to interact with the thyroid hormone receptor and retinoid X receptor-alpha. Two transcript variants encoding different isoforms have been found for this gene.
26S protease regulatory subunit 8
, 26S proteasome AAA-ATPase subunit RPT6
, proteasome 26S subunit ATPase 5
, proteasome subunit p45
, MSUG1 protein
, Tat-binding protein homolog 10
, proteasome 26S ATPase subunit 5
, thyroid hormone receptor-interacting protein 1
, thyroid receptor interactor 1
, for proteasomal ATPase (SUG1)
, peptidase (prosome, macropain) 26S subunit, ATPase 5
, protease (prosome, macropain) 26S subunit, ATPase 5
, proteasomal ATPase (SUG1)
, proteasome p45/SUG
, 26S protease subunit
, TAT-binding protein homolog 10
, SUG1 homolog