gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Adhesion regulating molecule 1

Adrm1, Rpn13, ARM-1, hRpn13
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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, UCH37, V1a, CAN, SET
Papers on Adrm1
ADRM1-amplified metastasis gene in gastric cancer.
Slamon et al., Baltimore, United States. In Genes Chromosomes Cancer, Jul 2015
UNASSIGNED: The proteasome ubiquitin receptor ADRM1 has been shown to be a driver for 20q13.3
A reversible and highly selective inhibitor of the proteasomal ubiquitin receptor rpn13 is toxic to multiple myeloma cells.
Kodadek et al., Jupiter, United States. In J Am Chem Soc, Jun 2015
Previously, Anchoori et al. identified Rpn13 as the target of an electrophilic compound (RA-190) that was selectively toxic to MM cells (Cancer Cell 2013, 24, 791-805), suggesting that this subunit of the proteasome is also a viable cancer drug target.
The E3 ubiquitin ligase parkin is recruited to the 26 S proteasome via the proteasomal ubiquitin receptor Rpn13.
Husnjak et al., Montréal, Canada. In J Biol Chem, Apr 2015
In our attempt to further elucidate the function of parkin, we have identified the proteasomal ubiquitin receptor Rpn13/ADRM1 as a parkin-interacting protein.
Structural plasticity allows UCH37 to be primed by RPN13 or locked down by INO80G.
Walters et al., Frederick, United States. In Mol Cell, Apr 2015
(2015),report crystal structures that define how deubiquitinating enzyme UCH37 is switched on or off by proteasome ubiquitin receptor RPN13 or chromatin remodeler component INO80G.
Mechanism of UCH-L5 activation and inhibition by DEUBAD domains in RPN13 and INO80G.
Sixma et al., Amsterdam, Netherlands. In Mol Cell, Apr 2015
In particular, the DUB UCH-L5 can be either activated or inhibited by conserved regulatory proteins RPN13 and INO80G, respectively.
Structural basis for the activation and inhibition of the UCH37 deubiquitylase.
Hill et al., Salt Lake City, United States. In Mol Cell, Apr 2015
We have performed biochemical characterization and determined crystal structures of UCH37 in complexes with RPN13 and NFRKB, which mediate its recruitment to the proteasome and INO80, respectively.
Knockdown of Adhesion-Regulating Molecule 1 Inhibits Proliferation in HL60 Cells.
Chen et al., Fuzhou, China. In Acta Haematol, 2014
BACKGROUND/AIMS: Adhesion-regulating molecule 1 (ADRM1), a receptor located on the 26S proteasome, is upregulated in many solid cancers.
A High Affinity hRpn2-Derived Peptide That Displaces Human Rpn13 from Proteasome in 293T Cells.
Walters et al., Frederick, United States. In Plos One, 2014
Rpn13 is a proteasome ubiquitin receptor that has emerged as a therapeutic target for human cancers.
The functional proteomics analysis of VEGF-treated human epithelial ovarian cancer cells.
Wu et al., Changsha, China. In Tumour Biol, 2014
A total of 17 expressed differential proteins were identified, 8 proteins were upregulated (ACTB, TIM, PDIA3, PDIA1, DCTN2, KIC17, SIAS, and KIC10) and 9 downregulated (KIC18, GRP78, CAPG, PPIA, ROA2, LMNA, EZRI, ADRM1, and ENOA).
ADRM1 gene amplification is a candidate driver for metastatic gastric cancers.
Kim et al., South Korea. In Clin Exp Metastasis, 2014
amplicon, ADRM1 was chosen for functional analyses.
Inherent asymmetry in the 26S proteasome is defined by the ubiquitin receptor RPN13.
Stanhill et al., Haifa, Israel. In J Biol Chem, 2014
Here, we show that although the vast majority (if not all) of the double-capped 26S proteasomes, both 19S complexes, contain the ubiquitin receptor Rpn10/S5a, only one of these 19S particles contains the additional ubiquitin receptor Rpn13, thereby defining asymmetry in the 26S proteasome.
A bis-benzylidine piperidone targeting proteasome ubiquitin receptor RPN13/ADRM1 as a therapy for cancer.
Roden et al., Baltimore, United States. In Cancer Cell, 2014
The bis-benzylidine piperidone RA190 covalently binds to cysteine 88 of ubiquitin receptor RPN13 in the 19S regulatory particle and inhibits proteasome function, triggering rapid accumulation of polyubiquitinated proteins.
Computational modeling suggests dimerization of equine infectious anemia virus Rev is required for RNA binding.
Carpenter et al., Ames, United States. In Retrovirology, 2013
EIAV Rev also contains a bipartite RNA binding domain comprising two short arginine-rich motifs (designated ARM-1 and ARM-2) spaced 79 residues apart in the amino acid sequence.
A possible connection between adhesion regulating molecule 1 overexpression and nuclear factor kappa B activity in hepatocarcinogenesis.
Yin et al., Changsha, China. In Oncol Rep, 2012
mRNA and protein levels of ADRM1 were increased in hepatocellular carcinoma tissues and was parallel to the metastatic potential
hRpn13, a newly identified component of the 19S particle, regulates proliferation, differentiation, and function in the human osteoblast-like cell line MG63. [corrected].
Tang et al., Chengdu, China. In J Physiol Biochem, 2012
hRpn13 modulates the influence of osteoblasts on osteoclasts by controlling the stability of regulatory proteins in osteoblasts.
Knockdown of ovarian cancer amplification target ADRM1 leads to downregulation of GIPC1 and upregulation of RECK.
Slamon et al., Los Angeles, United States. In Genes Chromosomes Cancer, 2011
this study provides a possible mechanism of action in ovarian cancer for amplification and overexpression of ADRM1
Phospho-ΔNp63α/Rpn13-dependent regulation of LKB1 degradation modulates autophagy in cancer cells.
Ratovitski et al., Baltimore, United States. In Aging (albany Ny), 2010
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.
The potential role of ubiquitin c-terminal hydrolases in oncogenesis.
Shen et al., Shanghai, China. In Biochim Biophys Acta, 2010
UCH-L1 possesses deubiquitinating activity and dimerization-dependent ubiquitin ligase activity, and functions as a mono-ubiquitin stabilizer; UCH-L3 does both deubiquitinating and deneddylating activity, except dimerization or ligase activity, and unlike UCH-L1, can interact with Lys48-linked Ub dimers to protect it from degradation and in the meanwhile to inhibit its hydrolase activity; UCH37 is responsible for the deubiquitinating activity in the 19S proteasome regulatory complex, and as indicated by the recent study, UCH37 is also associated with the human Ino80 chromatin-remodeling complex (hINO80) in the nucleus and can be activated via transient association of 19S regulatory particle- or proteasome-bound hRpn13 with hINO80; BAP1, binding to the wild-type BRCA1 RING finger domain, is regarded as a tumor suppressor, but for such suppressing activity, as demonstrated otherwise, both deubiquitinating activity and nucleus localization are required.
Regulators of the proteasome pathway, Uch37 and Rpn13, play distinct roles in mouse development.
Oravecz et al., The Woodlands, United States. In Plos One, 2009
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
Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1.
Cohen et al., Kansas City, United States. In Nat Cell Biol, 2006
Neither Uch37 alone nor the Uch37-Adrm1 or Uch37-Adrm1-S1 complexes can hydrolyse di-ubiquitin efficiently; rather, incorporation into the 19S complex is required to enable processing of polyubiquitin chains.
share on facebooktweetadd +1mail to friends