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Rpn13-Rpn2 complex structural analysis shows that RA190 targets hRpn13 and Uch37 through parallel mechanisms and at proteasomes, RA190-inactivated Uch37 cannot disassemble hRpn13-bound ubiquitin chains
findings indicate that up-regulated ADRM1 was involved in intrahepatic cholangiocarcinoma (ICC) progression and suggest the potential clinical application of ADRM1 inhibitors (e.g., RA190 and KDT-11) for ICC treatment.
We show that ADRM1 mRNA overexpression is an early event in high grade serous carcinoma of the ovary. This is associated with TP53 mutation and increased burden of misfolded proteins in carcinomas that likely renders the cancer cells particularly sensitive to RPN13 inhibitors.
evidence that the interaction can mediate the association of Rpn13 and SGTA in a cellular context.
The structures of proteasome substrate receptor complexes with the shuttle factors that deliver ubiquitinated proteins to proteasomes have been solved, namely human Rpn13 complexed with PLIC2 and Saccharomyces cerevisiae Rpn1 with Rad23.
RPN13 binds ubiquitin with an affinity similar to that of other proteasome-associated ubiquitin receptors and that RPN2, ubiquitin, and the deubiquitylase UCH37 bind to RPN13 with independent energetics.
regulation of NY-ESO-1 processing by the ubiquitin receptors Rpn10 and Rpn13 as a well as by the standard and immunoproteasome is governed by non-canonical ubiquitination on non-lysine sites.
this work implicates hRpn13 and Uch37 in cell cycle progression, providing a rationale for their function in cellular proliferation and for the apoptotic effect of the hRpn13-targeting molecule RA190.
the binding of SGTA to Rpn13 enables specific polypeptides to escape proteasomal degradation and/or selectively modulates substrate degradation.
Data suggest that ADRM1 is involved in proliferation of acute leukemia cells; expression of ADRM1 is up-regulated in leukemia; knockdown of ADRM1 inhibits cell proliferation at G0/G1 phase of cell cycle but does not affect apoptosis/cell migration.
findings implicate Rpn13 in linking parkin to the 26 S proteasome and regulating the clearance of mitochondrial proteins during mitophagy
Data show that DEUBAD domain in RPN13 (ADRM1) activates ubiquitin thioesterase L5 (UCH-L5), and the related DEUBAD domain in INO80G (NFRKB) inhibits UCH-L5.
Together, our findings suggest that the interaction of Psmd1 with Adrm1 is controlled by SUMOylation in a manner that may alter proteasome composition and function.
ADRM1 is a candidate target gene in the chromosome 20q13.33 amplicon that may possibly be linked to development of gastric cancer
Autoubiquitination of the 26S proteasome on Rpn13 regulates breakdown of ubiquitin conjugates.
Inherent asymmetry in the 26S proteasome is defined by the ubiquitin receptor RPN13.
mRNA and protein levels of ADRM1 were increased in hepatocellular carcinoma tissues and was parallel to the metastatic potential
hRpn13 modulates the influence of osteoblasts on osteoclasts by controlling the stability of regulatory proteins in osteoblasts.
this study provides a possible mechanism of action in ovarian cancer for amplification and overexpression of ADRM1
In tumor cells non-phosphorylated DeltaNp63alpha failed to form protein complexes with Rpn13, allowing the latter to bind and target LKB1 into a proteasome-dependent degradation pathway, modulating cisplatin-induced autophagy.
studies suggest that HAP40-mediated reduction of ADRM1 alters the mitochondrial fission activity and results in mitochondrial fragmentation and mitochondrial dysfunction.
Data show that either Rpn13 knock down or RA190 treatment reduced the capacity of myeloid-derived-suppressor cells (MDSCs) to suppress T cell proliferation in vitro.
this study showed that Rpn13 plays a redundant role with Rpn10 in recognition and degradation of ubiquitinated proteins in mouse livers.
this is the first report characterizing the physiological roles of Uch37 and Rpn13 in murine development and implicating a non-ATPase proteasomal protein, Rpn13, in the process of gametogenesis
show that Rpn13 is involved in inducible nitric oxide synthase degradation and is required for iNOS interaction with the deubiquitination protein UCH37.
ARM-1 is a cytosolic protein associated with the plasma membrane. However, no cell surface expression of the protein was observed. These results suggest an indirect role of ARM-1 in adhesion rather than a direct role as an adhesion molecule itself.
identification of a new ubiquitin receptor, Rpn13/ARM1, a known component of the proteasome
crystallography and NMR data to describe the ubiquitin-binding mechanism of Rpn13
The protein encoded by this gene is an integral plasma membrane protein which promotes cell adhesion. The encoded protein is thought to undergo O-linked glycosylation. Expression of this gene has been shown to be induced by gamma interferon in some cancer cells. Two transcript variants encoding the same protein have been found for this gene.
proteasomal ubiquitin receptor ADRM1
, adhesion regulating molecule 1
, ADRM1 protein
, 110 kDa cell membrane glycoprotein
, M(r) 110,000 surface antigen
, proteasome regulatory particle non-ATPase 13
, rpn13 homolog
, adhesion-regulating molecule 1
, glycoprotein 110
, cell membrane glycoprotein, 110000M(r) (surface antigen)
, adhesion regulating molecule 1a
, adhesion regulating molecule 1b